Structural invariants in protein folding.

C Chothia

doi:10.1038/254304a0

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Structural invariants in protein folding.

C Chothia

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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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Amino Acids Hydrogen Molecular Weight Protein Conformation Water Journal Article Research Support, U.S. Gov't, P.H.S.

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C Chothia. 1975-03-27. Structural invariants in protein folding.. https://doi.org/10.1038/254304a0

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