post #11 of 11
Originally Posted by F3AR View Post
I remember my biology teacher banging on about how the lock and key model is outdated and we use the induced fit now.

Not that it matters.
What they are saying is almost on the same line as induced fit. In induced fit, the substrate or key causes a change in the structure of the enzyme while binding.
Instead it seems they believe that the substrate is modified by the enzyme. Certainly plausible, not far fetched or anything. I'd imagine more of a combination of the two but we'll see with more research.

Originally Posted by MrDeodorant View Post
I wondered about that, but as I understand it (not being a folder myself, you understand), folding is about how a single protein fits itself together, and this is how two proteins interact with each other. Totally different.
While FAH is about how a single protein goes about the process of assuming it's secondary, tertiary and ultimately quaternary structure (if it's more than one polypeptide chain, or subunit), it is trying to figure out how the intermolecular forces and covalent bonds between the same polypeptide chain or different polypeptide chains interact and causes changes in structure.
These researchers are trying to figure out how a hole protein interacts with a substrate, generally a smaller protein or even a small polypeptide chain. The same intermolecular forces are at play here, as this is how enzyme substrate bind. They are trying to figure out how these intermolecular forces actually effect the binding and if there are any other factors at play here.

What I'm trying to explain, is that these are not totally different concepts. They are instead very similar and related concepts.