Conformational microstates proteins

Figure 1.6 Schematic representation of the changes in protein conformational microstate distribution that attend ligand (i.e., substrate, transition state, product and inhibitor) binding during enzyme catalysis. For each step of the reaction cycle, the distribution of conformational microstates is represented as a potential energy (PE) diagram.

Both the denaturation process in proteins and the melting transition (also referred to as the helix-to-coil transition) in nucleic acids have been modeled as a two-state transition, often referred to as the all-or-none or cooperative model. That is, the protein exists either in a completely folded or completely unfolded state, and the nucleic acid exists either as a fully ordered duplex or a fully dissociated monoplex. In both systems, the conformational flexibility, particularly in the high-temperature form, is great, so that numerous microstates associated with different conformers of the biopolymer are expected. However, the distinctions between the microstates are ignored and only the macrostates described earlier are considered. For small globular proteins and for some nucleic acid dissociation processes,11 the equilibrium between the two states can be represented as... 

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