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  • Problem Solving

How to Solve a Problem

Last Updated: April 3, 2023 Fact Checked

This article was co-authored by Rachel Clissold . Rachel Clissold is a Life Coach and Consultant in Sydney, Australia. With over six years of coaching experience and over 17 years of corporate training, Rachel specializes in helping business leaders move through internal roadblocks, gain more freedom and clarity, and optimize their company’s efficiency and productivity. Rachel uses a wide range of techniques including coaching, intuitive guidance, neuro-linguistic programming, and holistic biohacking to help clients overcome fear, break through limitations, and bring their epic visions to life. Rachel is an acclaimed Reiki Master Practitioner, Qualified practitioner in NLP, EFT, Hypnosis & Past Life Regression. She has created events with up to 500 people around Australia, United Kingdom, Bali, and Costa Rica. There are 12 references cited in this article, which can be found at the bottom of the page. This article has been fact-checked, ensuring the accuracy of any cited facts and confirming the authority of its sources. This article has been viewed 1,299,202 times.

How you deal with challenges will often determine your success and happiness. If you’re stuck on how to solve a problem, try defining it and breaking it into smaller pieces. Choose whether to approach the problem logically or whether you should think about how the outcome might make you feel. Find ways to creatively approach your problems by working with other people and approaching the problem from a different perspective.

Approaching the Problem

Step 1 Define the problem.

  • For example, if your room is constantly messy, the problem might not be that you’re a messy person. It might be that you lack containers or places to put your items in an organized way.
  • Try to be as clear and thorough as possible when defining the problem. If it is a personal issue, be honest with yourself as to the causes of the problem. If it is a logistics problem, determine exactly where and when the problem occurs.
  • Determine whether the problem is real or self-created. Do you need to solve this problem or is this about something you want? Putting things in perspective can help you navigate the problem-solving process.

Step 2 Make important decisions first.

  • For example, you might have several problems to solve and need to decide which ones to tackle first. Solving one problem may ease tension or take stress off of another problem.
  • Once you make a decision, don’t doubt yourself. Be willing to look forward from that point on without wondering what would have happened had you chosen something else.

Step 3 Simplify the problem.

  • For example, if you need to turn in many assignments to pass a class, focus on how many you have to do and approach them one by one.
  • Try to combine and solve problems together whenever possible. For example, if you're running out of time to study, try listening to a recorded lecture while walking to class or flip through note cards as you're waiting for dinner.

Rachel Clissold

  • For example, if you’re trying to pass a cumulative test, figure out what you already know and what you need to study for. Review everything you already know, then start learning more information from your notes, textbook, or other resources that may help you.

Step 5 Anticipate future outcomes.

  • Pay attention to know these scenarios make you feel.

Step 6 Allocate your resources.

  • For example, if you have a deadline, you may skip cooking dinner or going to the gym so that you can give that time to your project.
  • Cut down on unnecessary tasks whenever possible. For example, you might get your groceries delivered to you to save on shopping time. You can spend that time instead on other tasks.

Taking a Creative Approach

Step 1 Brainstorm different solutions.

  • If you’re making a complex decision, write down your alternatives. This way, you won’t forget any options and will be able to cross off any that aren’t plausible.
  • For example, you might be hungry and need something to eat. Think about whether you want to cook food, get fast food, order takeout, or sit down at a restaurant.

Step 2 Try different approaches to a problem.

  • Problems like accepting the job across the country that offers good pay but takes you away from your family may require different ways of approach. Consider the logical solution, but also consider your thoughts, feelings, and the way the decision affects others.

Step 3 Get advice from others.

  • For example, if you’re buying a home and not sure how to make your final decision, talk to other homeowners about their thoughts or regrets about buying a home.

Step 4 Monitor your progress.

  • For example, if you’re having financial difficulties, notice how your efforts are affecting the money coming in and the money you’re spending. If keeping a budget helps, keep with it. If using cash exclusively is a headache, try something else.
  • Keep a journal where you record your progress, successes, and challenges. You can look at this for motivation when you are feeling discouraged.

Managing Your Emotions While Confronting Difficulties

Step 1 Calm...

  • The first step is often the scariest. Try doing something small to start. For example, if you're trying to become more active, start going for daily walks.

Step 2 Address any underlying problems.

  • For example, if you’re overwhelmed by having a long to-do list, maybe the problems isn’t the list, but not saying “no” to things you can’t do.
  • If you're feeling stressed, angry, or overwhelmed, you may be burned out. Make a list of things that cause stress or frustration. Try to cut down on these in the future. If you start feeling overwhelmed again, it may be a sign that you need to cut back.

Step 3 Work with a therapist.

  • Find a therapist by calling your local mental health clinic or your insurance provider. You can also get a recommendation from a physician or friend.

Expert Q&A

Rachel Clissold

  • If you start feeling overwhelmed or frustrated, take a breather. Realize that every problem has a solution, but sometimes you're so wrapped up in it that you can't see anything but the problem. Thanks Helpful 0 Not Helpful 0
  • Don't turn away from your problems. It will come back sooner or later and it will be more difficult to solve. Common sense can help to reduce the size of the problem. Thanks Helpful 0 Not Helpful 0

how can we solve this problem brainly

You Might Also Like

Do Well in School

  • ↑ https://hbr.org/2017/06/how-you-define-the-problem-determines-whether-you-solve-it
  • ↑ https://www.cuesta.edu/student/resources/ssc/study_guides/critical_thinking/106_think_decisions.html
  • ↑ https://au.reachout.com/articles/a-step-by-step-guide-to-problem-solving
  • ↑ Rachel Clissold. Certified Life Coach. Expert Interview. 26 August 2020.
  • ↑ https://serc.carleton.edu/geoethics/Decision-Making
  • ↑ https://www.psychologytoday.com/blog/positive-psychology-in-the-classroom/201303/visualize-the-good-and-the-bad
  • ↑ https://www.britannica.com/topic/operations-research/Resource-allocation
  • ↑ https://www.niu.edu/citl/resources/guides/instructional-guide/brainstorming.shtml
  • ↑ https://www.healthywa.wa.gov.au/Articles/N_R/Problem-solving
  • ↑ https://www.collegetransfer.net/Home/ChangeSwitchTransfer/I-want-to/Earn-My-College-Degree/Overcoming-Obstacles
  • ↑ https://psychcentral.com/lib/5-ways-to-solve-all-your-problems/
  • ↑ https://www.apa.org/topics/psychotherapy/understanding

About This Article

Rachel Clissold

To solve a problem, start by brainstorming and writing down any solutions you can think of. Then, go through your list of solutions and cross off any that aren't plausible. Once you know what realistic options you have, choose one of them that makes the most sense for your situation. If the solution is long or complex, try breaking it up into smaller, more manageable steps so you don't get overwhelmed. Then, focus on one step at a time until you've solved your problem. To learn how to manage your emotions when you're solving a particularly difficult problem, scroll down. Did this summary help you? Yes No

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How to Counter Waste Disposal Challenges in Every Scale

Woman carrying a garbage bag in the kitchen

Yes, that candy wrapper you threw on the ground the other day can have lasting effects on the environment.

Waste disposal problems have become a pressing issue for many countries, and it has become a global problem everyone needs to address. Since 2015, there are at least 5.25 trillion pieces of plastic in the oceans, and these can be dangerous to the wildlife that comes across it. And did you know that the solution for many developed countries is to send their waste to developing countries ?

At this point, it’s not enough to look at waste management and disposal as a problem global leaders and local governments have to deal with. The extreme waste problem we’re facing right now started because everyday people like you and me thought one candy wrapper left on the ground or one plastic bottle left on a park bench was not going to make a dent in the amount of waste their area makes. But when hundreds of millions of people share this mindset, it becomes dangerous as the waste starts to accumulate.

Whether it is plastic, an old computer, or your worn-out shoes, you have to think about the appropriate waste management and disposal. Waste disposal is a lengthy but methodical process that includes burial, burning, recycling, discharge, and other processes.  Indeed, many organizations and localities in the world are grappling with the problem, unable to handle it completely. Here are some common  waste disposal problems in various scales and potential solutions.

Waste Management at Home

waste management stats

The average American tosses out at least 4.4 pounds (almost 2 kilograms) of trash every day. Try to think back yesterday to all the things you threw away. These could include food containers, single-use plastics for household items, bottles, or even food scraps. But when you consider the total population in the United States, you’re looking at at least 728,000 tons (around 660 million kilograms) per day. Just try to imagine 63,000 garbage trucks dumping a full load into a landfill – that’s roughly how much waste is made a day.

It’s going to be difficult to go from 4.4 pounds of trash per day to becoming like those eco-friendly vloggers that can fit years’ worth of waste into one regular mason jar. But you have to at least start somewhere when it comes to making your household more eco-friendly . Here are a few solutions that can help you reduce the amount of waste you put in your trash.

Turn Away from Single-Use Plastics

A few examples of these include plastic straws (there are plenty of reusable alternatives like glass and metal straws or biodegradable options like plant-based, bamboo, or paper straws), sanitary napkins (switch to reusable menstrual cups), and take-out containers (if ordering take-out, see if they provide biodegradable containers or bring your own reusable containers and ask the restaurant to put your food in there).

One good way of doing this is by shopping at bulk stores and zero-waste stores that provide products without packaging. You can opt to bring your own reusable containers or purchase reusable containers from their store.

Avoiding single-use plastic may mean having to change your lifestyle. This may include buying shampoo bars or shampoos from bulk stores to avoid buying shampoos in bottles, or shopping at a farmer’s market for produce instead of your local supermarket to avoid buying produce that’s wrapped in plastic and styrofoam.

Sort Your Garbage

Investing in more garbage containers can help you sort out your waste. There’s a general color coding for garbage containers to sort out waste easier, but if your local garbage collector doesn’t sort their trash and tosses them all in the same truck, then there really isn’t a point to following these colors. Instead, just get any trash receptacles and follow sorting procedures you and your household can follow.

In my household, for example, our local garbage collector doesn’t sort trash and just dumps it. So, what we do is we separate plastic bottles, metal waste, and fruits and vegetable scraps from our everyday waste. I’ll let you know what we do with the food scraps below, but for plastic and metal waste, we clean them and place them in separate bins. Once we’ve filled up our recyclable bins, we take them to local recycling centers.

segregating the trash

Sort Your Scraps

You can avoid wasting your food scraps and leaving them to rot in landfills by reusing scraps. I’ve studied how to compost, so whenever I have biodegradable waste that can be used to compost, I take it and add it to my composting bin. It’s a great way to reduce the amount of waste I make in a day while finding a better use for those scraps.

Extreme & Hazardous Waste

Outside your home, however, waste poses a serious problem to your community. A problem grappling organizations is the production of too much waste. When countries are producing 220 million tons of waste annually , then you know there is a big problem. Now, imagine the amount being produced cumulatively across the globe. The consumerism shown by producers and companies is coming back to haunt us.

Waste management services are on their toes as they seek ways to take care of hazardous waste. The fact that most of the waste nowadays is toxic is posing a huge challenge, yet manufacturing companies continue to increase their production. The companies are producing products every day and there is a chance some of the toxic waste will end up in the environment.

The U.S. EPA once reported that the number of untested chemicals in homes is around 60,000. Plastic toys contain Biphenyl-A (BPA), which is a hazardous chemical. As the amount of solid waste continues to increase, we can only expect a harder challenge of dealing with toxic waste disposal.

Show Support for Eco-Friendly Movements

Support zero-waste stores and businesses like bulk stores that are centered around reducing waste. Consumer trends are changing, and now that the millennial and Gen Z age groups are poised to become one of the largest consumer groups in the next few years, making your business eco-friendly and sustainable can attract a large percent of these age groups that prefer doing business with greener small businesses.

Landfill Problems

Truck unloading garbage at a landfill

Monitoring laxity on the side of laws and regulations is also proving to be a huge hindrance to landfill management. Toxicity increases to levels that become unmanageable for decades.

Conventional Technologies

It is becoming apparent that some technologies are no longer applicable to modern waste reduction and recycling, yet some organizations continue to rely on them. These technologies offer quick but short-term solutions, a reason they continue to be popular in some areas. However, more technology is also evolving or being created to solve waste management problems.

Technology can be used to recycle or upcycle waste, create alternatives from products that normally produce more waste, or find a way to address the ever-growing problem of waste management. Tech Insider shows plenty of these types of tech, including plastic-free shampoo pods and toothpaste pills, machines that sustainably remove waste from bodies of water, or finding ways to recycle materials like plastic.

Solutions to Waste Disposal Challenges

There are many cost-effective ways of solving the above problems, including the popular ‘Reduce, Reuse, Recycle’ approach. Local communities must be educated on this form of waste management that deals with unsustainable waste excellently. Techniques such as repairing a broken chair instead of buying a new one can go a long way in countering the problem.

Alongside responsibility, it is crucial for local authorities to embrace modern waste disposal, with gradual improvements as the catch. In line with that, control of landfilling is necessary. Items that can be reclaimed or recycled should not be allowed to stand in the landfill.

But most of all, waste management cannot be possible without the help of everyday people changing their waste management practices at home. While it’s true that corporate waste also contributes to the total waste that’s plaguing our environment, people can start to reduce their waste in the comfort of their own home. It may require making conscious changes to their lifestyle, but it’s necessary if we want to see the changes in the amount of waste the average person produces in one day.

The reality is that we can achieve proper waste disposal, but it won’t be easy. Adopting modern ways of doing things and focusing on long-term plans will eventually yield the desired results. Policy support is definitely irreplaceable in tackling the global problem of waste disposal and management.

About The Author

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Alex Miller

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  • Published: 12 January 2021

Structural biology in the fight against COVID-19

  • Montserrat Bárcena 1 ,
  • Christopher O. Barnes 2 ,
  • Martin Beck 3 ,
  • Pamela J. Bjorkman 2 ,
  • Bruno Canard 4 ,
  • George F. Gao 5 ,
  • Yunyun Gao 6 ,
  • Rolf Hilgenfeld 7 ,
  • Gerhard Hummer 3 ,
  • Ardan Patwardhan 8 ,
  • Gianluca Santoni 9 ,
  • Erica Ollmann Saphire 10 ,
  • Christiane Schaffitzel 11 ,
  • Sharon L. Schendel 10 ,
  • Janet L. Smith 12 ,
  • Andrea Thorn 6 ,
  • David Veesler 13 ,
  • Peijun Zhang 14 , 15 &
  • Qiang Zhou 16 , 17  

Nature Structural & Molecular Biology volume  28 ,  pages 2–7 ( 2021 ) Cite this article

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  • Cryoelectron microscopy
  • X-ray crystallography

How can structural biology help us understand and combat SARS-CoV-2? Researchers in the field share their experiences and opinions and point to the challenges that lie ahead.

Since the release of the SARS-CoV-2 genomic sequence in January 2020, structural biologists have been hard at work to reach a molecular and atomic understanding of this insidious virus. Despite disruptions and restrictions due to pandemic lockdowns, they have generated a high volume of data and scientific articles. They have also put considerable effort into peer reviewing manuscripts and project proposals on the topic. Nevertheless, several of those researchers have carved time out of their busy schedules to contribute to this Feature and tell us about the role of structural biology in the fight against SARS-CoV-2 and other emerging viral diseases, the technological developments that have allowed such rapid progress, and future directions for the field.

Montserrat Bárcena

Elucidating the structure and function of viral proteins is essential to understand the mechanisms of viral replication and pathogenesis and, therefore, to pave the way for new antiviral strategies. In the last five years, cryo-EM has become a fundamental pillar of structural virology thanks to improvements in detectors and automation. The many SARS-CoV-2-related structures solved by cryo-EM and single-particle analysis during the ongoing pandemic illustrate the maturity of cryo-EM as a structural technique for suspensions of molecules.

how can we solve this problem brainly

Viral infection, however, is inextricably linked to the host cell. That is where viruses use their full range of tricks to manipulate the cell and to replicate. Bringing structural virology to this natural battlefield is the next step forward. This goal has been greatly facilitated by the recent development of focused ion beam (FIB) milling to prepare thin cellular samples suitable for cryo-tomography. Cellular cryo-tomography allows the structural analysis of viral and host players in situ. It can also unveil new viral complexes, such as the molecular pore in the coronavirus replication organelle, which we recently described 1 . These cryo-tomograms also provide a wealth of information about the cellular context, but new tools for data analysis, mining and sharing are required to fully explore this information. Although cellular cryo-tomography currently provides relatively low-resolution data, there is no fundamental reason why near-atomic resolutions could not be achieved if it were combined with subtomogram averaging. The current technical bottlenecks are the low-throughput sample preparation and data collection steps. During the next few years, these hurdles will surely be overcome, as they are the focus of extensive ongoing developments aimed to increase automation and reproducibility. In my view, once it reaches its full potential, cellular cryo-tomography is destined to be the next cryo-EM revolution and may critically reshape our understanding of viral infection.

Christopher O. Barnes and Pamela J. Bjorkman

In less than a year, researchers have uncovered structure–function details for many of the proteins encoded by SARS-CoV-2, the virus responsible for the current global pandemic. Remarkably, structures of the SARS-CoV-2 spike trimer were published in March 2020, only about two months after the viral sequence was available, aided by previous studies that established how to stabilize coronavirus spikes and the rapid turnaround time for solving structures by single-particle cryo-EM. Since then, other structures have revealed how spike binds to its angiotensin-converting enzyme 2 (ACE2) receptor, the specificities of polyclonal antibody responses in COVID-19-convalescent individuals, and how monoclonal neutralizing antibodies or designed protein inhibitors bind spike to prevent infection.

how can we solve this problem brainly

Collectively, these structures provide the foundation for the development of potential therapeutics. For example, they will allow pairs of monoclonal antibodies to be chosen for treatment cocktails, they will improve antibody potencies through structure-based engineering so that they are effective at lower doses and/or are resistant to viral mutations, and they will facilitate epitope mapping to guide structure-based immunogen design. With respect to facilitating immunogen design, current candidate vaccines against SARS-CoV-2 in clinical trials did not require extensive structural biology information; however, the identification of conserved epitopes and subsequent structures of antibodies bound to spikes from SARS-CoV-2 and related coronaviruses in animal reservoirs could enable the design of immunogens to elicit cross-reactive protection against future emerging coronaviruses with pandemic potential.

how can we solve this problem brainly

A major challenge to this approach will be focusing the immune response on an epitope or epitopes that induce antibodies with neutralizing activity across multiple viral strains, an obstacle shared with HIV-1 immunogen design. With structural information and improved biochemical methods to mask distracting epitopes, a pan-neutralizing vaccine protecting against multiple coronaviruses may be attainable. Overall, structural biology is a valuable tool to gather information that will aid us in controlling the current pandemic and future outbreaks of deadly viruses.

Martin Beck and Gerhard Hummer

Spike, the SARS-CoV-2 surface protein, mediates host-cell entry and is the major target of neutralizing antibodies and vaccine development. This intriguing molecular machine displays exceptional structural dynamics, both to carry out its functions and to evade the immune system. Three hinges in the long stalk between the body and the viral membrane render spike flexible to an extent not reported for other viral envelope proteins. The stalk itself contains an unusual right-handed coiled coil that may be metastable. Whether the hinges provide avidity to enhance cellular entry or comprise a mechanical sensor to promote conformational transitions remains unknown.

how can we solve this problem brainly

This structural plasticity extends to the receptor-binding domain (RBD), where transitions from closed to open states enable spike to bind human ACE2. Proteolytic cleavage by host proteins and low pH further activate spike, trigger the shedding of the S1 subunit, expose the fusion peptide and enable the dramatic conformational reorganization into the so-called post-fusion structure that drives membrane fusion and infection through a not yet fully understood mechanism.

Conformational dynamics renders spike dangerous at all stages of the infection process. Its mobile glycans shield spike from neutralizing antibodies. Dynamic clustering of spike on the viral surface combined with stalk flexibility may enhance viral avidity by allowing multiple spikes to engage with host receptors. RBD activation appears to be quasi-irreversible and can be triggered by a wide range of stimuli. Of particular concern is weak antibodies that may induce this activating transition by conformational selection, while being unable to neutralize the virus. This process may add a new twist to ‘antibody-dependent enhancement,’ which is normally associated with increased endocytic uptake, but here it may be amplified by nonspecific activation of spike’s spring-loaded fusion machinery. Further in situ structural analysis, particularly of the actual infection events, will be important to address these questions in detail.

how can we solve this problem brainly

Bruno Canard

Viral diagnostics, antiviral drugs, vaccines: progress in these areas would be much slower without structural biology. Rapid developments in coronavirus (CoV) research demonstrate this point. Before 2003, only a single CoV protein structure was available in the wwPDB — that of the main protease of transmissible gastroenteritis virus (TGEV). The emergence of SARS-CoV, the first highly pathogenic human CoV, launched an intense international effort to combat the virus at the time. Modeling and molecular replacement approaches using the TGEV data yielded structural information for the SARS-CoV main protease in record time, demonstrating the power of structural biology to expedite molecular insights into emerging pathogens. The nascent era of viral structural genomics advanced and contributed, in less than a decade, to the elucidation of the majority of the structures of CoV proteins, making SARS-CoV one of the best understood viruses at the structural level.

how can we solve this problem brainly

The importance of high-resolution cryo-EM cannot be understated. Before 2016, crystal structures of individual CoV proteins and protein domains dominated. Out of 550 SARS CoV and SARS-CoV-2 PDB entries today, more than 180 were determined after 2016; 90% of these are structures of SARS-CoV-2 proteins deposited in 2020 alone. Cryo-EM accelerated considerably the pace of discovery for structures of large proteins and protein complexes, which would have been very difficult to solve using crystallography. Interestingly, overcoming future roadblocks may depend on journal editorial boards as well as on further technical advances. It is important that journals ensure reports of cryo-EM structures are accompanied by solid biochemical characterization. In addition, we need to generate functional and mechanistic data that complement the still images provided by three-dimensional (3D) structures, for example, by using the X-ray free-electron laser and other time-resolved techniques.

Virology is of course much broader than CoV biology. A number of important human viral pathogens are waiting to be as thoroughly investigated as those of Coronaviridae. The impressive achievements made on the latter will certainly translate to the former. As next-generation DNA and RNA sequencing techniques have undergone their own technical revolution, structural and functional metagenomics of the virosphere may become the next frontier.

George F. Gao

The late structural biologist and crystallographer Don C. Wiley, who was my mentor at Harvard University, used to say “Get another pair of glasses to ‘see’ the biology by using structural biology methods.” To me, that is the beauty of structural biology in contributing to our understanding of life. Trained initially as a veterinarian, I worked on animal microbiology and infectious diseases for my MSc degree and entered the field of virology and immunology during my DPhil and postdoctoral training. I have recently become involved in public health more generally, including global health strategy and public health administration. Throughout my career, I have realized how structural biology indeed helps open our eyes so we can see biology unfolding 2 and shapes the biomedical research field. Studies on antigenic peptide presentation by the major histocompatibility complex (MHC) have delineated T cell–based immunity, allowing us to clearly view and confirm hypotheses. Research on receptor–ligand interactions helps us view the host immune response in action as well as viral entry into host cells and has led to the development of small molecules and biological drugs for disease treatments. In fact, structural biology has made drug development faster than ever.

how can we solve this problem brainly

When COVID-19 emerged at the end of 2019 (ref. 3 ), structural biologists immediately got to work and, using crystallography and cryo-EM, quickly defined the mechanisms of virus entry, with structures of the envelope spike protein in complex with its cellular receptor, including those from my own group, quickly published. Researchers also provided information on the main viral enzyme activities to drive inhibitor development, for example, targeting its replication machinery. In retrospect, it is clear that structural biology has played key roles in the research and development of prophylactic and therapeutic agents against many emerging and re-emerging pathogens, such as Ebola, Zika and HIV, among others.

With SARS-CoV-2, scientists and public health workers have witnessed up close the devastating toll caused by this particularly covert virus, but much remains to be learned about its biology. Though interdisciplinary efforts have increased recently, we still need more scientists who are trained in both structural and cell biology, with strong physics and biology backgrounds, as this combination of skills will enable more problem-solving-oriented research. I believe this field will be booming and will bring new research paradigm changes.

Yunyun Gao, Gianluca Santoni and Andrea Thorn

As developers of structural biology methods, we usually work far from the spotlight: we are the expert users, the problem solvers, the workshop teachers and software developers, not the biologists chasing cures. When the COVID-19 pandemic began, we asked ourselves how we could contribute to the fight against the virus and established the Coronavirus Structural Task Force 4 .

how can we solve this problem brainly

As early as February 2020, we started evaluating the SARS-CoV structures available in the wwPDB and realized that many could be considerably improved. We quickly set up a website and a database containing our evaluation and revised models. Within a week, aided by other methods developers from across the world, we began to systematically examine all published SARS-CoV structures and the new SARS-CoV-2 structures. Soon there were 25 of us — mostly postdocs and undergraduate and graduate students — meeting online every day, working on automatic structure evaluation and revising individual structures using newly developed tools and, of course, making all of our findings available online. We also engaged in outreach activities, writing blog posts about the structural biology of SARS-CoV-2 aimed at both the scientific community and the general public, refining structures live on Twitch and offering a 3D printable virus model for schools.

how can we solve this problem brainly

We contacted the original authors of the structures that we were able to improve, which led not only to revisions of structures in the wwPDB but also to preprints being corrected before publication. Suddenly, we were being contacted by downstream users, including individual labs as well as large initiatives (such as Folding@Home, OpenPandemics and the EU-JEDI challenge) focused on quickly finding treatments for SARS-CoV-2. The media also got wind of our work, which was covered in articles and interviews on radio and TV and in newspapers and internet outlets.

There were no tenured academics in the Task Force; we were an ad hoc collaboration of mostly junior researchers across nine time zones, brought together by a common desire to fight the pandemic. We lacked management experience, computing facilities and administrative infrastructure. Nevertheless, we were able to rapidly establish a large network of COVID-19-related research, forge friendships and collaborations across national boundaries and provide improved models for multiple in silico drug discovery projects.

how can we solve this problem brainly

Following this initial burst of activity, we can now begin to assess its impact: we hope to have made a real difference in the fight against COVID-19, both scientifically and in improving the public’s understanding of the virus and of scientists’ efforts. We also hope that our efforts will be recognized by our peers and senior colleagues and that our decision to make all of our work rapidly and freely available will not be detrimental to our careers, since high-impact papers are the usual metric by which scientists are evaluated. We hope that the Coronavirus Structural Task Force will be a useful model for rapid, collaborative responses to pressing societal challenges.

Rolf Hilgenfeld

Structural biology analyses of coronaviruses did not begin with the current SARS-CoV-2 pandemic but started in 2002 and 2003, when we reported the first crystal structures of coronavirus family proteins, namely, the main proteases (M pro ) of transmissible gastroenteritis virus (TGEV) and human coronavirus 229E 5 , 6 . Since then, 3D structures of the spike protein, the nucleocapsid and most of the 16 non-structural proteins of SARS-CoV and other coronaviruses have been determined. Some of those structures provided important clues about the function of the non-structural proteins. Because of the high sequence similarity between SARS-CoV and SARS-CoV-2 proteins, researchers were able to rely on a solid body of structural data when SARS-CoV-2, the new coronavirus causing the current COVID-19 pandemic, emerged in early 2020.

how can we solve this problem brainly

In addition to providing insights into the function of coronaviral proteins, structures are important for the design of antiviral therapeutics. One of the most prominent targets for such compounds is coronaviral M pro . From the start, we used our early M pro structures to design and synthesize inhibitors 6 . More recently, we synthesized and tested benzotriazoles and α,β-unsaturated esters as M pro blockers, followed by α-ketoamides. Combining structural biology with medicinal chemistry in the same laboratory was a successful strategy, as almost no one will know the structure of the target better than the scientist who determined it. It gives me immense pleasure to design small-molecule inhibitors based on crystal structures determined by my group — creating a new molecule is clearly different from analyzing the structure of its target, and I encourage structural biologists to integrate medicinal chemistry into their efforts.

Ardan Patwardhan

The proliferation of cryo-EM studies in structural biology has led to concomitant increases in depositions to the structural archives — the EMDB (for 3D volumes), EMPIAR (for image data) and the PDB (for atomic models). The EMDB reached a milestone in February 2020 with its 10,000th released entry. We anticipated a slowdown due to the pandemic shutdowns but, to the contrary, depositions have continued at pace: as of 10 November 2020, there were 213 EMDB entries related to SARS-CoV-2 from 70 publications and 12 EMPIAR entries from 9 publications. The viral spike protein has the highest number of entries (168 in the EMDB), followed by the RNA-dependent RNA polymerase, although the diversity of sample types has grown over time.

how can we solve this problem brainly

There is a need for improved validation of cryo-EM maps and models and for improvements to and expansion of the data and metadata collected to enable validation. We also need to be able to effectively deal with the increasing complexity of cryo-EM experiments, which result in equally complex multimap and multimodel depositions. All of these challenges have been highlighted by community experts as requiring urgent attention, for example, at the Wellcome Trust UK EM Validation Network (WT-EM-VALNET) “Frontiers in cryo-EM validation” (January 2019) and the wwPDB single-particle EM data management (January 2020) workshops. With the added urgency of the pandemic and the pressure to rapidly publish and make SARS-CoV-2 structures available to the public, it is perhaps understandable that there may be a greater preponderance of issues with those entries (for example, modeling errors or maps and models that are described in a paper but not deposited). On the other hand, it could simply be that these structures have been more scrutinized than most; this became evident at the recent WT-EM-VALNET Zoomposium “Cryo-EM Validation in the Age of SARS-CoV-2,” as many different groups (for example, the Coronavirus Structural Task Force coalition) have been carefully examining and rerefining atomic models.

In the future, it would be useful for all of the stakeholders involved, including the organizations running the archives, journal publishers, funding agencies and the structural community, to leverage the experience from SARS-CoV-2 to improve policies and procedures for structural data archiving. For example, one idea is to ask authors to provide a table with their manuscript listing all figure parts depicting maps and/or models along with their respective accession codes. This would greatly facilitate the review process and ensure that no map or model depositions get missed, while providing greater clarity to readers wanting to delve deeper by examining the entries. Another idea is to move toward a routine deposition of some form of image data (at least the particle stacks corresponding to EMDB map depositions) to EMPIAR to enable recalculation of the map.

Christiane Schaffitzel

Structural and computational biology play key roles in elucidating the molecular mechanisms of disease phenotypes and in driving drug discovery. This is exemplified by the current fast-paced efforts to respond to the COVID-19 pandemic. To aid these endeavors, the University of Bristol set up the COVID Emergency Group (UNCOVER), coordinated by Bristol clinician Adam Finn, which initiated multidisciplinary collaborations among virologists, chemists, physicians, pharmacologists and others to accelerate our understanding of COVID-19 and to design tailored treatments urgently needed to overcome the crisis. In our work, we discovered a druggable pocket in the SARS-CoV-2 spike glycoprotein, the viral component that mediates the interaction with ACE2 and that is essential for infection 7 . In our cryo-EM structure of spike, this pocket was occupied by linoleic acid (LA), an essential polyunsaturated free fatty acid (FFA). LA stabilized spike in a locked conformation that is incompatible with ACE2 binding and is thus considered ‘non-infective.’ Intriguingly, LA synergizes with remdesivir, the first drug approved for COVID-19 treatment, to block viral replication in cells 7 .

how can we solve this problem brainly

Our discovery has actionable implications: the data suggest that LA could act as a prophylactic antiviral. Intriguingly, sera from patients with COVID-19 have decreased levels of FFAs, including LA 8 ; therefore, LA supplementation may be beneficial. Small molecules binding the FFA-binding pocket (LA mimics) have potential as future antivirals, as they may lock spike in a non-infective conformation. Finally, the body metabolizes LA to eicosanoids, including prostaglandin, which are key molecules in immune modulation. In addition, LA-based phospholipids maintain the fluidity of cell membranes and surface tension in the lung. While more research is required to decipher the interplay of FFAs, SARS-CoV-2 and COVID-19 pathology, targeting the LA metabolic axis could help prevent rampant inflammatory responses in severe cases of COVID-19 and reduce respiratory distress and the risk of pneumonia in patients.

Sharon L. Schendel and Erica Ollmann Saphire

At no time in history have we been better able to image our viral enemies and launch immune defenses than now. The availability of direct electron detection, coupled with advanced instrumentation for selecting and analyzing cells of interest, lays at our feet a wealth of stunning detail and paves the route forward for medical defenses. Advances in cryo-EM instrumentation and data analysis freed us from the need to screen thousands of crystals and shrank the time needed to produce structures from years to days. Moreover, we can now begin to capture the structural and temporal heterogeneity and flexibility through which actual biology is manifested. Our new ability to detect subtle differences in glycosylation and antibody occupancy can further guide therapeutic development. We can precisely analyze structures of uniform monoclonal antibodies in a delivered therapeutic as well as the breadth of antibodies in the polyclonal milieu of actual patients.

how can we solve this problem brainly

We are harnessing these new capabilities in collaborative efforts to characterize the features of antibodies that best correlate with the ability to protect living things. La Jolla Institute for Immunology (LJI) is the headquarters for two global consortia to discover antibody-based therapeutics: one group is focused on SARS-CoV-2 and the other on re-emerging threats like Ebola, Lassa and chikungunya. Dozens of contributors provided antibodies against these viruses to be analyzed side-by-side to reveal multiple parallel facets of antibody function. We will pair results from these analyses with structural studies to define, in exquisite detail, how antibodies act to provide protection against deadly viral infections. Together, the speed and illumination of our instrumentation and the biophysical, biochemical and immunological information gained through collaboration fill gaps in knowledge and allow us to claim new victories in the fight against infectious disease

how can we solve this problem brainly

Janet Smith

Three-dimensional structures of macromolecules are the basis for much of our understanding of the molecular aspects of pathogenesis. With structures, we can explain pathogen resistance to antibiotic and antiviral drugs, the transfer of proteins and DNA into foreign cells, and the membrane fusion events that lead to infection by viruses such as influenza, HIV-1 and SARS-CoV-2. Structural biology has also greatly advanced our knowledge of the molecular pathways of the innate and adaptive immune systems. Ribosome structural biology is being used to develop new antibiotics, and RNA structures, together with an atomic-level understanding of translation, have led to the development of new RNA-based vaccines. Our lab’s structural studies of the flavivirus NS1 protein fostered a new understanding of the function of this enigmatic virulence factor. NS1 was found to have a previously unknown role in virus packaging and to induce the vascular leak that is a hallmark of severe dengue disease. The structure opened new possibilities for the development of antivirals and vaccines against dengue, Zika, West Nile and other flaviviruses.

how can we solve this problem brainly

The speed and reach of structure determination have increased due to many technological advances, for example, hot microbeams at synchrotron sources for crystallography; high-speed, low-noise detectors for electron microscopy and crystallography; and faster, cheaper computing for all methods. These and other advances put the ‘biology’ in structural biology, allowing structural knowledge to be prospective rather than retrospective. Nowhere is this more apparent than in the response of the research community to the COVID-19 pandemic. In the first ten months following the publication of the SARS-CoV-2 genome sequence, the PDB released more than 560 structures of viral proteins and RNA from researchers around the world (72% of the structures were from crystallography, 27% from cryo-EM and 1% from NMR). These are a foundation for vaccine and antiviral development efforts and for new discoveries in the basic biology of both host and pathogen.

David Veesler

The recent emergence of a previously unknown coronavirus (designated SARS-CoV-2) resulted in the ongoing COVID-19 pandemic, which has claimed over 1.2 million lives and brought the world to a standstill. On 10 January 2020, the first genome sequence of a SARS-CoV-2 isolate was made publicly available and initiated the race to understand the molecular architecture and functional intricacies of this new pathogen. Cryo-EM structures of the SARS-CoV-2 spike glycoprotein and of the RNA-dependent RNA polymerase, along with crystal structures of the spike receptor-binding domain in complex with its host receptor, ACE2, were determined in just a few weeks. These results provided blueprints of the viral infection and replication machineries, which have been used by thousands of researchers worldwide for the design of vaccines and viral inhibitors. Structures of the spike glycoprotein ectodomain revealed the conformational dynamics of the receptor-binding domain, alternatively exposing and masking the ACE2-interaction site in a manner reminiscent of what had been previously observed for SARS-CoV and MERS-CoV and was postulated to contribute to immune evasion. Cryo-ET studies of fixed SARS-CoV-2 revealed the marked flexibility of full-length spike trimers relative to the viral membrane, along with the supramolecular organization of this pleiomorphic virus.

how can we solve this problem brainly

A wave of spike glycoprotein structures in complex with antibodies yielded insights into the host humoral immune response to SARS-CoV-2 infection and delineated an antigenic map of the receptor-binding domain, which accounts for most of the neutralizing activity in COVID-19 convalescent plasma. Past and present single-particle cryo-EM studies have enabled the engineering of spike trimers with altered conformation and enhanced stability and informed the rational design of the unprecedentedly large number of protein subunit, nucleic acid and viral vector vaccines currently in development. Finally, structural biology has supported the development and uncovered the mechanism of action of computationally designed ultrapotent miniprotein inhibitors of viral entry, heralding a new era for the rapid development of prophylactic and therapeutic countermeasures against emerging pathogens.

Peijun Zhang

In response to the COVID-19 pandemic, efforts from scientists around the world have yielded a great deal of knowledge on the etiological agent, SARS-CoV-2. Structural understanding of the viral components is key to the development of therapeutics and, so far, work has concentrated on viral spikes, the major protease, RNA polymerase and other non-structural proteins, as well as interactions between spike and ACE2 and neutralizing antibodies. Researchers have used a range of tools, from synchrotron-based X-ray crystallography to cryo-EM and cryo-ET. The last two techniques are essential for in vitro and in situ study to obtain information in the context of a virion. All of these techniques will be important in tackling the challenges that lie ahead — including the structural elucidation of the remaining viral components, such as N, E, and M proteins and ribonucleoproteins, which are small, flexible and heterogeneous, and in some cases membrane bound — and they will be pivotal in understanding the entire virus architecture and its genome organization.

how can we solve this problem brainly

Much less is known about the SARS-CoV-2 replicative cycle in the native cellular environment. Viral genome replication, assembly and egress is a multistage process that is critically important, as it comprises multiple targets for medical interventions to stop infection. We have recently developed a unique correlative multimodal, multiscale cryo-imaging approach, combining in cellulo soft X-ray cryo-tomography and serial cryo-focused ion beam/scanning electron microscope volume imaging of the entire near-native SARS-CoV-2-infected cell, with high-resolution cryo-ET and subtomogram averaging of individual components. This approach enables a holistic view of the infection process, from the level of the whole cell to individual molecules, revealing not only the cytopathic effects of SARS-CoV-2 infection but also new pathways of SARS-CoV-2 assembly and egress. Further development in the area of labeling individual viral and host proteins involved in the process will be essential to allow a correlative structural analysis at the molecular level.

SARS-CoV-2 is the seventh coronavirus known to infect humans and has caused the COVID-19 pandemic. SARS-CoV-2 shares 80% sequence identity with SARS-CoV, responsible for the 2002–2003 SARS epidemic. Both coronaviruses use ACE2 to invade cells and cause similar symptoms, but SARS-CoV-2 has much higher infectivity.

how can we solve this problem brainly

Structural biology has an essential role in antiviral research for SARS-CoV-2. Structures for almost all of the important antiviral targets, including the spike protein, the main protease and the RNA-dependent RNA polymerase, have been determined. Those studies have benefited from the ‘resolution revolution’ in single-particle cryo-EM, which has greatly improved the efficiency of structure determination. Within two months of the outbreak, structures of spike and its complex with ACE2 were determined, laying the foundation for subsequent studies of the invasion mechanism and for the development of antiviral drugs, neutralizing antibodies and vaccines.

The huge impact of the pandemic has driven many structural biologists to participate in SARS-CoV-2-related research as much as possible, pushing the field into new territory. At present, there are hundreds of entries in the wwPDB related to SARS-CoV-2; a large fraction involves small molecules and neutralizing antibodies that could potentially be used for antiviral treatment. The advances in cryo-ET technology have enabled direct visualization of the architecture of SARS-CoV-2 virion particles, opening the door for in situ structural biology.

Since the beginning of the 21st century, frequent and periodic outbreaks of infectious diseases caused by viruses have become the norm. Developing specific drugs for such diseases is an urgent need and poses a great challenge. The progress of structural biology, and especially of cryo-EM technology, will empower antiviral drug development and help combat viral diseases.

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California Institute of Technology, Pasadena, CA, USA

Christopher O. Barnes & Pamela J. Bjorkman

Max Planck Institute of Biophysics, Frankfurt am Main, Germany

Martin Beck & Gerhard Hummer

Centre National de la Recherche Scientifique and Aix-Marseille University, Marseille, France

CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China

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Institute of Molecular Medicine, University of Lübeck, Lübeck, Germany

European Molecular Biology Laboratory (EMBL-EBI) European Bioinformatics Institute, Hinxton, UK

European Synchrotron Radiation Facility, Grenoble, France

Gianluca Santoni

Center for Infectious Disease and Vaccine Research, La Jolla Institute for Immunology, La Jolla, CA, USA

Erica Ollmann Saphire & Sharon L. Schendel

School of Biochemistry and Bristol Synthetic Biology Centre (BrisSynBio), University of Bristol, Bristol, UK

Life Sciences Institute and Department of Biological Chemistry, University of Michigan, Ann Arbor, MI, USA

Janet L. Smith

University of Washington, Seattle, WA, USA

Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK

Diamond Light Source, Harwell Science and Innovation Campus, Didcot, UK

Center for Infectious Disease Research, Westlake Laboratory of Life Sciences and Biomedicine, Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, China

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C.S. declares that patent applications describing methods and material compositions based on the presented observations have been filed. D.V. is a consultant for Vir Biotechnology Inc. The Veesler laboratory has received a sponsored research agreement from Vir Biotechnology Inc. All other authors declare no competing interests.

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Bárcena, M., Barnes, C.O., Beck, M. et al. Structural biology in the fight against COVID-19. Nat Struct Mol Biol 28 , 2–7 (2021). https://doi.org/10.1038/s41594-020-00544-8

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Published : 12 January 2021

Issue Date : January 2021

DOI : https://doi.org/10.1038/s41594-020-00544-8

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200-year-old geology mystery resolved

  • Kate McAlpine

To build mountains from dolomite, a common mineral, it must periodically dissolve. This counter-intuitive lesson could help make new defect-free semiconductors and more.

Two men holding rocks stand in a computer laboratory. The man on the left is wearing black-rimmed glasses and a navy blue blazer over a white shirt with fine black stripes. He also holds two palm-sized, light-pink rocks in each hand. The man on the right is holding a larger, light-pink rock over his head and is wearing a gray sweater.

For 200 years, scientists have failed to grow a common mineral in the laboratory under the conditions believed to have formed it naturally. Now, a team of researchers from the University of Michigan and Hokkaido University in Sapporo, Japan have finally pulled it off, thanks to a new theory developed from atomic simulations.

Their success resolves a long-standing geology mystery called the “Dolomite Problem.” Dolomite—a key mineral in the Dolomite mountains in Italy, Niagara Falls, the White Cliffs of Dover and Utah’s Hoodoos—is very abundant in rocks older than 100 million years , but nearly absent in younger formations.

“If we understand how dolomite grows in nature, we might learn new strategies to promote the crystal growth of modern technological materials,” said Wenhao Sun , the Dow Early Career Professor of Materials Science and Engineering at U-M and the corresponding author of the paper published today in Science.

The secret to finally growing dolomite in the lab was removing defects in the mineral structure as it grows. When minerals form in water, atoms usually deposit neatly onto an edge of the growing crystal surface. However, the growth edge of dolomite consists of alternating rows of calcium and magnesium. In water, calcium and magnesium will randomly attach to the growing dolomite crystal, often lodging into the wrong spot and creating defects that prevent additional layers of dolomite from forming. This disorder slows dolomite growth to a crawl, meaning it would take 10 million years to make just one layer of ordered dolomite.

Wenhao's open palms are in sharp focus and take up nearly all of the image. The rest of Wenhao's body is barely visible. He is holding three rocks, one in his right hand, two more in his left. The rocks are a motley of reddish-pink, reddish-brown, and black colors, with some white showing wear the edges have worn.

Luckily, these defects aren’t locked in place. Because the disordered atoms are less stable than atoms in the correct position, they are the first to dissolve when the mineral is washed with water. Repeatedly rinsing away these defects—for example, with rain or tidal cycles—allows a dolomite layer to form in only a matter of years. Over geologic time, mountains of dolomite can accumulate.

To simulate dolomite growth accurately, the researchers needed to calculate how strongly or loosely atoms will attach to an existing dolomite surface. The most accurate simulations require the energy of every single interaction between electrons and atoms in the growing crystal. Such exhaustive calculations usually require huge amounts of computing power, but software developed at U-M’s Predictive Structure Materials Science (PRISMS) Center offered a shortcut.

“Our software calculates the energy for some atomic arrangements, then extrapolates to predict the energies for other arrangements based on the symmetry of the crystal structure,” said Brian Puchala , one of the software’s lead developers and an associate research scientist in U-M’s Department of Materials Science and Engineering.

A layer of perfectly alternating and diagonal rows of blue and orange spheres are interspaces with rows of black spheres. Another identical layer of spheres sits below the first, and is visible on the right-hand side of the top layer, which is incomplete. The spheres represent the constituent atoms that comprise a dolomite crystal.

That shortcut made it feasible to simulate dolomite growth over geologic timescales.

“Each atomic step would normally take over 5,000 CPU hours on a supercomputer. Now, we can do the same calculation in 2 milliseconds on a desktop,” said Joonsoo Kim, a doctoral student of materials science and engineering and the study’s first author.

The few areas where dolomite forms today intermittently flood and later dry out, which aligns well with Sun and Kim’s theory. But such evidence alone wasn’t enough to be fully convincing. Enter Yuki Kimura , a professor of materials science from Hokkaido University, and Tomoya Yamazaki , a postdoctoral researcher in Kimura’s lab. They tested the new theory with a quirk of transmission electron microscopes.

“Electron microscopes usually use electron beams just to image samples,” Kimura said. “However, the beam can also split water, which makes acid that can cause crystals to dissolve. Usually this is bad for imaging, but in this case, dissolution is exactly what we wanted.”

The transmission electron microscope is a long, tan device standing upright on a black desk. Several knobs and attachments protrude from the instrument, and a collection of wires connect the device to a computer panel on the right-hand side of the microscope.

After placing a tiny dolomite crystal in a solution of calcium and magnesium, Kimura and Yamazaki gently pulsed the electron beam 4,000 times over two hours, dissolving away the defects. After the pulses, dolomite was seen to grow approximately 100 nanometers—around 250,000 times smaller than an inch. Although this was only 300 layers of dolomite, never had more than five layers of dolomite been grown in the lab before.

The lessons learned from the Dolomite Problem can help engineers manufacture higher-quality materials for semiconductors, solar panels, batteries and other tech.

“In the past, crystal growers who wanted to make materials without defects would try to grow them really slowly,” Sun said. “Our theory shows that you can grow defect-free materials quickly, if you periodically dissolve the defects away during growth.”

The research was funded by the American Chemical Society PRF New Doctoral Investigator grant, the U.S. Department of Energy and the Japanese Society for the Promotion of Science.

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What is Q*? And when we will hear more?

The cats out of the bag. Reuters published. Any interpretations? Any knowledge files out there on the subject?

Definitely makes me question Sam’s motives and puts the recent drama in a different light.

This is moving towards more existential questions, faster than anyone imagined, and I’d rather not have Microsoft, Larry Summers or the ex-CEO of fricking Salesforce making the calls whether or not something is AGI.

It’s shades of ‘repealing Glass-Steagall’ to leave it up to those w/ a literal vested interest in keeping AI commercially-viable to make the call whether AGI has been achieved.

One does not mistakenly keep board members ‘out of the loop’ re: discovering AGI and possibly the biggest breakthrough in human civilization

Can of worms for sure… Real time! I wonder what I will wake up to tomorrow. But the currant chatter feels like ripple echos to me. Probably an announcement on Q* before Christmas.

Exclusive: OpenAI researchers warned board of AI breakthrough ahead of CEO ouster -sources | Reuters .

The maker of ChatGPT had made progress on Q* (pronounced Q-Star), which some internally believe could be a breakthrough in the startup’s search for superintelligence, also known as artificial general intelligence (AGI), one of the people told Reuters. OpenAI defines AGI as AI systems that are smarter than humans.

As someone who’s done a fair amount of ML/AI research, I can tell you that it is very very easy to think you’ve discovered a breakthrough.

There is a great deal of cognitive bias in AI, and you have to falsify very aggressively.

I am deeply skeptical.

It’s also worth noting that in the news today we found out that the 86B share-sale is back on. I’m sure this ‘breakthrough’ will get investors quite interested.

Separately, a person familiar with the matter told The Verge that the board never received a letter about such a breakthrough and that the company’s research progress didn’t play a role in Altman’s sudden firing.

It wouldn’t be a bad time to start thinking about community AI boards to start the alignment aspects of the transition we face. The last week gives us clues to what we could expect in the future. Uncharted territory.

Q-learning is an algorithm that helps an agent learn the best actions to take in a given state to maximize a reward.

That’s it pretty much

I believe the ongoing discussions are less about AGI itself and more about concerns regarding leadership decisions and safety protocols. AGI has the potential to revolutionize every aspect of society, and it’s crucial that we prepare for its impact across all spheres of humanity. It represents a pivotal key—with one turn, it could unlock tremendous benefits or pose significant risks. Ensuring that robust safety measures are in place is essential.

The leaders in the field, including Sam and other directors, are tasked with navigating this complex landscape. I trust they are doing their utmost to secure a safe transition into this new era. We will reach our goals with AGI, but let’s proceed with the necessary precautions—better safe than sorry in the realm of transformative technologies.

I did an eval on q-learning “way back” when gpt-4 was released!

I never had the time to fully finish it and I might’ve got some stuff wrong.

Was it a basic algo of high school mathematics and better rewards ?



Some interesting ideas on how to use q-learning to train LLMs.

The first idea matches a bit with the synthetic data comments we are hearing.

Interactive Learning Environment: Q-learning requires an environment where it can interact and receive feedback. For LLMs, this could be a simulated or real-world interface where the model can perform tasks, ask questions, or engage in dialogues and receive rewards based on the quality and relevance of its responses or actions.

I would argue that intelligence is smart enough to not fall for the wiles of short-term goals. With the firm grasp the ChatGPTs had of ethics, I would argue we are in good hands.

AGI will be achieved in the next 6 - 24 months. It is inevitable and it would be better to prepare for it now than trying to stop it (which is a futile effort) and may mean other less well meaning actors will be in charge of humanities most powerful invention ever to exist, and perhaps something that turns out to be the most most advanced evolutionary species since human beings

IF and only IF the Q* mentioned is the same.

I don’t think that’s true. NLP is widely considered to be the main barrier to achieving AGI. OpenAI’s success in the area caused me and many others to think we could see AGI within a couple of years. I’ve been telling people for months that they should shorten their mental time frames from years to months. I don’t mean that I think AGI will happen that quickly; I just mean that advancements we thought were years away are now happening on an almost weekly basis.

So, if the Reuters article is true, it’s not surprising. If we haven’t had a breakthrough with AGI already, then we almost certainly will soon.

From deepmind, some cute bot animations and a good visual explanation

It’s robotics, but transformers are the basis of LLMs.


My goal is to get a q* post ‘community flagged’. That will be a sign!

Heh. Must be tough working at such a core company that could potentially have a very broad impact on humanity. All that kibitizing…

Don’t worry folks, the 86B+ share sale should help a bit.

The acronym RACE - Real-time Antiquation of Current Ecosystem , meaning everything you make, AI will break is about right here.

Every advancement that OpenAI makes implementation of the current AI out of date. I remember watching Khan Academy describe their education platform saying ‘This AI will watch this AI’ - that’s basically agents, but the way they probably implemented it was probably much different and very expensive to build. Autogen / Assistants made that simple.

The paradigm of building AI applications is different than other tech. Every time you finish building a lunar rocket for $10bn just as you apply the paintwork, there are rockets available in Walmart for $9.99m - but can get to Mars, ( deployable living pods, Sirius XM, leatherette seats and aircon extra.)

Given this reality of building. What is your thoughts on a) Technical implementation b) Business strategy

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F1 News: McLaren Pinpoints "Priority" For 2024 - "Seem To Lose Competitiveness"

Posted: November 24, 2023 | Last updated: November 24, 2023

The McLaren Racing team has revealed that it can no longer ignore the low downforce problem on its MCL60 F1 car, a phenomenon that causes the car's aerodynamics to switch off at low downforce levels. Solving the issue is a high-priority task for the team for 2024.

Despite making considerable gains in performance in the second half of this season to emerge as one of Red Bull's serious challengers, a challenging episode during the Las Vegas Grand Prix hinted that the rival teams were better prepared in their cars' low downforce setup. 

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Considering the rise in the number of circuits on the calendar that demand a low downforce setup, McLaren cannot afford to lose points next season due to a peculiar low downforce problem in their cars. 

Team boss Andrea Stella revealed that the team's data hinted at a loss of performance in low downforce scenarios compared to rival teams. He told the media:

“We seem to lose competitiveness when we need to run the car at this drag level. “We do see, when it comes to our own observations, the fact that the aerodynamics kind of tends to switch off. “I'm sure that's the same for everyone, but it's more about how large this phenomenon is – and it would look like it is slightly higher for our car than for some of our competitors.” 

Increase In Low Downforce Circuits

Stella also added that the addition of tracks like Baku and Vegas to the F1 calendar meant that the team could not afford to ignore the problem. He added:

“While we continue with the development at the medium/high downforce with what we have done this year, we have definitely added quite a lot of work at low downforce and we want to go prepared to these circuits. “Now with Baku, with Vegas, Monza, and Spa, it starts to become a decent number of races for which you do have to have an optimised car. “In the past, it was only Spa/Monza. So now we have added a few more races, it's a priority.” 

Highlighting the technical side of the story, Stella added that the cars' aerodynamics become quite sensitive causing them to lose downforce in a non-linear way. He explained:

“When you go for a low rear wing, you go with a low front wing [for balance reasons], and very often this influences both ends because, when you reduce the load on the front wing, you reduce control of the front wheel wake. “That affects then the behaviour of the car. “So rather than simply losing [downforce] linearly, there's a point in which you lose more than linearly. And that's what you would like to bring back to kind of a linear loss.” 

Just ahead of the Las Vegas GP, the Woking outfit created an ultra-low downforce setup that features a single beam wing element but eventually opted out of using it because of the low grip nature of the new track. Stella concluded:

“We had a new rear wing flap. "We had another option to run even lower drag with the beam wing, but we didn't use it because we thought that we needed to leave some downforce on the car because of the low tarmac grip. So, we just used one of the two upgrades we had. “But certainly, we knew that this kind of upgrade doesn't change the personality of the car in terms of how it responds to the rear wing level, and we knew that this was going to be a bit of a struggle.”

F1 News: McLaren Pinpoints "Priority" For 2024 - "Seem To Lose Competitiveness"

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