Abstract

It is argued that simplified models capture key features of protein stability and folding, whereas more detailed models may be more appropriate for protein structure prediction. A brief overview of experimental and theoretical results is presented that corroborates these points. I argue that statistical models capture the key principle of protein stability-cooperativity- and therefore provide a reasonable estimate of protein free energy whereas more detailed but less physically transparent calculations fail to do so. I also explain that the previously published claim that simple models give predictions that are inconsistent with experiments on polypeptide block-copolymers is based on incomplete analysis of such experiment.

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