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Biophys Chem. 1997 Jan 31;63(2-3):97-105.

Protein folding and wring resonances.

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Physics Department, Building 307, The Technical University of Denmark, DK-2800 Lyngby, Denmark.


The polypeptide chain of a protein is shown to obey topological constraints which enable long range excitations in the form of wring modes of the protein backbone. Wring modes of proteins of specific lengths can therefore resonate with molecular modes present in the cell. It is suggested that protein folding takes place when the amplitude of a wring excitation becomes so large that it is energetically favorable to bend the protein backbone. The condition under which such structural transformations can occur is found, and it is shown that both cold and hot denaturation (the unfolding of proteins) are natural consequences of the suggested wring mode model. Native (folded) proteins are found to possess an intrinsic standing wring mode.


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