TL;DRAbstract
For a typical protein, the global stability at room temperature is of the order 10 kcal/mol ∼20 kBT for a ∼100 residue domain. Thus proteins are stabilized with a free energy of a fraction of kBT per amino acid. Nonetheless, proteins have well-defined structures that are stabilized by cooperative interactions between their many small parts. Thus there is essentially no “partial melting” of the protein; it stays folded and specifically functional to do whatever job it is supposed to do. When a large enough fluctuation does indeed melt the protein, the structure can (mostly) reassemble.
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For a typical protein, the global stability at room temperature is of the order 10 kcal/mol ∼20 kBT for a ∼100 residue domain. Thus proteins are stabilized with a free energy of a fraction of kBT per amino acid. Nonetheless, proteins have well-defined structures that are stabilized by cooperative interactions between their many small parts. Thus there is essentially no “partial melting” of the protein; it stays folded and specifically functional to do whatever job it is supposed to do. When a large enough fluctuation does indeed melt the protein, the structure can (mostly) reassemble.
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