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Structural invariants in protein folding

Naturevolume 254pages304308 (1975) | Download Citation

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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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Author notes

    • Cyrus Chothia

    Present address: Service de Biochimie cellulaire, Institut Pasteur, 28, rue du Docteur Roux, 75015, Paris, France

Affiliations

  1. Department of Chemical Physics, The Weizman Institute of Science, Rehovot, Israel

    • Cyrus Chothia
  2. MRC Laboratory of Molecular Biology, Hill, Road, Cambridge, UK

    • Cyrus Chothia

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https://doi.org/10.1038/254304a0

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