Protein folding and wring resonances

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

The polypeptide chain of a protein is shown to obey topological contraints 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.
Original languageEnglish
JournalBiophysical Chemistry
Volume63
Pages (from-to)97-105
ISSN0301-4622
Publication statusPublished - 1997

Cite this

@article{3b0c74832a4542859359efc206e2c1d9,
title = "Protein folding and wring resonances",
abstract = "The polypeptide chain of a protein is shown to obey topological contraints 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.",
author = "Jakob Bohr and Henrik Bohr and S{\o}ren Brunak",
year = "1997",
language = "English",
volume = "63",
pages = "97--105",
journal = "Biophysical Chemistry",
issn = "0301-4622",
publisher = "Elsevier",

}

Protein folding and wring resonances. / Bohr, Jakob; Bohr, Henrik; Brunak, Søren.

In: Biophysical Chemistry, Vol. 63, 1997, p. 97-105.

Research output: Contribution to journalJournal articleResearchpeer-review

TY - JOUR

T1 - Protein folding and wring resonances

AU - Bohr, Jakob

AU - Bohr, Henrik

AU - Brunak, Søren

PY - 1997

Y1 - 1997

N2 - The polypeptide chain of a protein is shown to obey topological contraints 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.

AB - The polypeptide chain of a protein is shown to obey topological contraints 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.

M3 - Journal article

VL - 63

SP - 97

EP - 105

JO - Biophysical Chemistry

JF - Biophysical Chemistry

SN - 0301-4622

ER -