The role of protein-solvent interactions in protein unfolding

The role of protein-solvent interactions in protein unfolding Protein unfolding occurs when the balance of forces between the protein's interaction with itself and the protein's interaction with its environment is disrupted. The disruption of this balance water structure around the protein. A decrease in the normal water—water interaction will result in an increase in the relative interaction of water with the protein. An increase in the number of interactions between water and the protein may initiate a protein's unfolding. This model for protein unfolding is supported by a range of recent experimental and computational data. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Current Opinion in Biotechnology Elsevier

The role of protein-solvent interactions in protein unfolding

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Publisher
Elsevier
Copyright
Copyright © 1996 Elsevier Ltd
ISSN
0958-1669
DOI
10.1016/S0958-1669(96)80119-4
Publisher site
See Article on Publisher Site

Abstract

Protein unfolding occurs when the balance of forces between the protein's interaction with itself and the protein's interaction with its environment is disrupted. The disruption of this balance water structure around the protein. A decrease in the normal water—water interaction will result in an increase in the relative interaction of water with the protein. An increase in the number of interactions between water and the protein may initiate a protein's unfolding. This model for protein unfolding is supported by a range of recent experimental and computational data.

Journal

Current Opinion in BiotechnologyElsevier

Published: Aug 1, 1996

References

  • The thermodynamic stability of proteins
    Schellman, JA
  • The molten globule state
    Ptitsyn, OB
  • The control of protein stability and association by weak interactions with water: how do solvents affect these processes?
    Timasheff, SN
  • Theoretical studies of protein folding and unfolding
    Karplus, M; Šali, A
  • Molecular dynamics simulations of protein unfolding and limited refolding: characterization of partially unfolded states of ubiquitin in 60% methanol and in water
    Alonso, DOV; Daggett, V
  • The effect of environment on the stability of an integral membrane helix: molecular dynamics simulations of surfactant protein C in chloroform, methanol and water
    Kovacs, H; Mark, AE; Johansson, J; Van Gunsteren, WF
  • Acid and thermal denaturation of barnase investigated by molecular dynamics simulations
    Caflisch, A; Karplus, M
  • A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding
    Arcus, VL; Vuilleumier, S; Freund, SMV; Bycroft, M; Fersht, AR

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