Abstract
An analysis of 15 protein structures indicates: First, the loss of accessible surface area by monomeric proteins on folding—proportional to hydrophobic energy—is a simple function of molecular weight; second, the proportion of polar groups forming intramolecular hydrogen bonds is constant; and third, protein interiors are closely packed, each residue occupying the same volume as it does in crystals of amino acids.
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Chothia, C. Structural invariants in protein folding. Nature 254, 304–308 (1975). https://doi.org/10.1038/254304a0
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DOI: https://doi.org/10.1038/254304a0
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