Structural invariants in protein folding
- 1 March 1975
- journal article
- Published by Springer Nature in Nature
- Vol. 254 (5498) , 304-308
- https://doi.org/10.1038/254304a0
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.Keywords
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