Origin of the Native Driving Force for Protein Folding

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چکیده

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Origin of the native driving force for protein folding.

We derive an expression with four adjustable parameters that reproduces well the 20x20 Miyazawa-Jernigan potential matrix extracted from known protein structures. The numerical values of the parameters can be approximately computed from the surface tension of water, water-screened dipole interactions between residues and water and among residues, and average exposures of residues in folded prot...

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Origin of Native Driving Force in Protein Folding

We derive an expression with four adjustable parameters that reproduces well the 20×20 MiyazawaJernigan potential matrix extracted from known protein structures. The numerical values of the parameters can be approximately computed from the surface tension of water, water-screened dipole interactions between residues and water and among residues, and average exposures of residues in folded prote...

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Protein folding: complex potential for the driving force in a two-dimensional space of collective variables.

Using the Helmholtz decomposition of the vector field of folding fluxes in a two-dimensional space of collective variables, a potential of the driving force for protein folding is introduced. The potential has two components. One component is responsible for the source and sink of the folding flows, which represent respectively, the unfolded states and the native state of the protein, and the o...

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Nature of Driving Force for Protein Folding -- A Result From Analyzing the Statistical Potential

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ژورنال

عنوان ژورنال: Physical Review Letters

سال: 2000

ISSN: 0031-9007,1079-7114

DOI: 10.1103/physrevlett.84.574