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On “Levinthal paradox” and the theory of protein folding

Authors
Journal
Journal of Molecular Structure THEOCHEM
0166-1280
Publisher
Elsevier
Publication Date
Volume
424
Identifiers
DOI: 10.1016/s0166-1280(97)00238-8
Keywords
  • Protein Folding Theory
  • Potential Hypersurface
Disciplines
  • Biology
  • Chemistry
  • Computer Science
  • Physics

Abstract

Abstract A general model of protein folding is proposed that links together concepts from molecular physics, thermodynamics and chemical kinetics. The model is based on a description of the potential hypersurface through a three-level taxonomy: conformational substates, conformational states, and free-energy levels. The required parameters are either estimated or taken from experimental or computational literature data. The free-energy barriers between conformational states are shown to be essentially negentropic in the folding direction. A consistent picture emerges, which answers Levinthal's paradox. It consists in a biased random walk with a very high degree of percolation. Finally, the model leads to a sketch of a possible algorithm for an ab initio simulation of protein folding.

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