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Aren't these discoveries supposed to be a little more mature before being awarded a Nobel? Admittedly, it works pretty well at predicting structure but no one just runs with the results without confirming the structure with crystallography, right?

:marseycope: from the /r/chemistry thread

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That's literally just because sc*entists are r-slurred and think there's a magical, god-given distinction between """real""" experiments and computation.

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Computation gives you a theoretical model and nice pretty curves. They still need to be considered academic.

Running actual experiments validates models and refines them. But it also introduces discrepancies which force you to improve laboratory procedures, develop more refined equipment, or you discover a new fundamental truth which explains the discrepancy.

  • "Why the frick is Uranus so weird?"

  • do theoretical math

  • "There's probably another planet out there messing up its orbit due to gravity and shit, and mathematically it must be X far away and by Z mass."

  • "Yep there it is"

That's why you combine theory and practice.

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Another r-slur who just handwaves "there's actual experiments which are different from theory because they just are okay????"

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If actual experiments differ from theory, that just means the theory needs to be updated.

Some stuff in physics matches REALLY well, particularly quantum physics. Like Feynman would always brag that for a few key quantities, the theoretical value and experimental values only differed by like 0.0000000000001%.

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That's still stuck in this same r-slurred mindset that "actual experiments" have priority over theory, simulation, etc. Scientists question ur assumptions instead of accepting dogma uncritically all the time challenge IMPOSSIBLE

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No it's not, it's just clear fact.

The purpose of theory is to predict reality. If it doesn't match the reality we can directly measure, then it won't match the reality we can't (or simply don't want to for cost etc reasons).

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>"Actual experiments" are REALITY and computer simulations aren't because THEY JUST AREN'T OKAY???

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I don't even know what you're pissed about at this point tbh bb. I never said computer simulations are worthless. In fact, if they match experimental results closely, that means you can extend the computer simulations to predict what will happen in reality. Which is really the whole purpose of science.

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KEYLOGGER

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:ipgrabber:

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The bread crumbs are piling up. After some tracking I found your IP: 141.11.191.246

Out of luck, son (snap)

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Case in point

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!ifrickinglovescience !chemistry !biology is Borpa (a biochem) right on the Soyentism question?

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Yes kill all scientagicians (this is a fusion of the words "scientist" and "magician", implying that scientists are a lot like magicians.)

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the entire point of science is doing math to try and predict observation, then adjusting math to fit it better (or adjusting observation instruments/methods to be more accurate). Without observation you don't have science.

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Literally uncritically regurgitated dogma lol worse than religioncels

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@SpookyBorpa is doing an r-slur's impersonation of Kuhn (maybe with a pinch of Popper) insinuating that interpreting experimental data, or even deciding what experiment to perform in the first place, is impossible outside of some theoretical framework, therefore doing an X-Ray crystallography on some protein you synthesized is just as prone to failing to predict its actual properties as simulating it on a computer (it's not obviously, let's hope that borpa's baiting and not a literal r-slur).

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The only phil of science this STEMcel knows is Popper and Kuhn, what a classic 😂😂😂 FYI both are completely irrelevant for contemporary phil of science and questions about the epistemic status of non-physical experiments. It's completely uncontroversial (in phil of science departments (aka smarter ppl than STEMcels)) that computer simulations create the same kind of evidence that """actual experiments""" do

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LMAO does this person really not understand why computational models of protein structure are useful?

Hint: if you want to create a molecule that has some desirable characteristics, it's a lot better to run a computer simulation over 1000 designs and physically test the most promising one, than to physically test all 1000.

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So far, that approach hasn't really borne fruit. It may in the future, but so far it still works better just to do a giant screen and see what hits.

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How do you choose which drugs to screen, considering there are far more options that you can afford to test?

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Round up more hobos, dummy.

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High throughput can scan thousands of compounds. Typically you would run compounds you already know work, some that have similar characteristics, some that have very different characteristics, and some that work for other purposes. They are typically extremely small amounts of natural products for each sample so pretty cheap and fast.

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You have billions of possible options, How do you choose a batch of several thousand from that?

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They are usually compounds known to be safe in humans. Huge libraries exist of either natural products or medications for other diseases. You can also take a compound you know binds to a certain protein or receptor and get crystallography data to determine what would best fit in the binding pocket. You don't need the best possible option, you just need a starting point for synthesis of derivatives.

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There are giant libraries of "drug-like" molecules that you use. They tend to be biased towards molecules that are easy to make by chemical manufacturers, which yes, is a problem. When a new good reaction comes along you'll often get new classes of compounds out of that. Depending on your target, you know what's had some interaction in the past, so you start with stuff that looks like that.

Once you get a hit or several, the compound isn't good enough as-is, so you start modifying it. In theory, computations could help you here as well, and maybe it's starting to, I don't know. Start making chemical modifications, see what helps it hit the target better. Of course, it has to do other stuff too: get into the target organs, not degrade too quickly, not be too toxic. There's various things you can try to make each of those better, but it's still largely guess-and-check. And usually it doesn't work. There's a reason that new medicine is expensive: it needs to not only pay for its own R&D, but also the R&D of everything that hasn't panned out.

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People don't even confirm a chemical compound with GC retention time without an orthogonal column or a Mass Spec.

Are redditors actually r-slurred?

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https://i.rdrama.net/images/17286075511497712.webp

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>can split drops from a buret with 1x10^-6 mL accuracy

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no, in this case it's contrarian dramatards who are. as of yet nothing useful has come out of it (one reason to get a nobel) and it's not really groundbreaking on the theoretical side (other reason to get a nobel). In 10 years it will most likely have the former but as of now it's mostly used to get mid science past peer review (ask me how I know :marseygiggle:)

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