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The best model I’ve come up for it, is to imagine how helpful it would be if locks attracted the key that could be used to unlock them.

Because the scales are so small, the charge amounts for the attraction and repulsions are minute, but real.

Granted, I’m self taught on all of this, so there will likely be objections to this simplification, but at the end of the day, it’s all about moving electrons around.

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I'm concerned that it would be irresponsible to answer your question because you might attempt some of these methods. A few days ago you were asking whether it was a good idea to dry your pantry by pouring sodium hydroxide into a corner. (Just to be clear, the answer is NO.)

These substances can be safely dried by people with appropriate equipment, knowledge, common sense, and oversight. You have demonstrated none of these. If you attempt to dry sodium hydroxide at home, by any method, you will create a damaging chemical accident. If you are interested in chemistry, and you enjoy having an intact home, two functional eyes, and a clean criminal record, please stop asking these questions on Reddit and go take a class at your local community college, or anywhere else that you can receive the education you need in a safe and supervised environment.

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Induced fit or conformational selection seems to be the two explanations with the most backing.

In induced fit, binding of the ligand changes the shape of the protein.

In conformational selection, the protein samples a number of different shapes, a subset of which is compatible with ligand binding.

I tend to think that "induced fit" is essentially conformational selection. All molecules seem to "breathe" to an extent, ie. small-scale movements between atoms (you can see this on structures in PyMol by looking at the B-factor) so this makes the most sense.

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It is sadly, OP has been banned. Please if you have doubts report the comment and we can have a look in more details.

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Viruses select nothing.

A random mutation happen in a virus genome.

if this new mutation doesn't give the virus any advantage compared to the other viruses => this mutation won't be spread since there are far more viruses with the "wild type" genotype.

if this new mutation give the virus an advantage (infectious advantage, hide immune system advantage, cell control advantage, speed of replication advantage....) => this mutation will spread for the next generations of viruses since this virus has something the wild type viruses don't have that makes him more efficient in his "life" cycle.

All mutations are neutral until the context gives the holder of this mutation a positive or negative selection.

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This reads like a ChatGPT answer for some reason.

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Static cling is part of it

Amino acids are arranged in a 3d matrix that creates a patch or a pocket with a particular pattern of positive and negative charges that complement a pattern of charges on the other molecule (the ligand). There's are also interactions involving hydrophobic vs hydrophilic molecular affinities, as well as overall physical shape.

When binding occurs, the interactions can induce changes in the overall shape of the binding site, as these different charges are "neutralized" against each other, or the two molecules adjust themselves for a better fit. This can sometimes result in the exposure of and otherwise hidden amino acid that can cause some further interaction to occur. There are also ways in which an amino acid nearby in the structure might pull electrons away from some part of the ligand, changing the properties of the molecule in a way that might cause it to break a bond. Breaking the amino acid chain in the ligand can then cause the other interactions holding it to the receptor to change, making the two parts no longer compatible with the receptor, allowing it to release .

I am leaving a whole lot of stuff out, but this is an idea that I find to be easier to visualize .

There are some types of locks which use and arrangement of magnets. The north and south poles of the different magnets are set up in a pattern that is complementary to the arrangement in the magnetic key. And so when you put the key next to the lock it can open, but if you put the wrong key next to the lock it will not be able to bind correctly. This is actually not a bad way to look at the interaction of receptors and their ligands or enzymes and their substrates.

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For understanding the idea the lock*key model works very well I think. I mean, it gets hard if you take into acount that most ligands don't bind covalently and attach/detach based on chemical properties that we -for simplicity's sake- call affinity. It brings in a lot of very specific kinetics that aren't usefull for understanding the basic concepts.

If OP goes deeper into biochemistry those factors will start to play a role and will be introduced bit by bit to keep it doable. A reddit post isn't really the place for that level of detail imho.

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MdmA is far from a miracle drug, but it does allow some one to open up more and talk about themself. It also ease the bond between people. Since therapy need to start with a bond of trust between the patient and the professional, it accelerate the treatment.

Ketamine is very fascinating, from what I remember, because the effect last longer than the drug. It allow some new neural connection, which help to change how one perceived the world. Ketamine in itself is not the solution, but it make it easier to help some one to get out of depression, since it is easier to change the way you perceived the world.

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