A sequence function reveals new features in beta-protein folding.

Hui Shao; Zong-Hao Zeng

doi:10.2174/0929866033478690

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A sequence function reveals new features in beta-protein folding.

Hui Shao·Zong-Hao Zeng

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Abstract

When amino acid residues are represented by parameters describing their side chain lengths and polarities, a sequence function defined as the sum of the first two sequence autocorrelation functions is found to be negatively and linearly correlated with the logarithms of folding rates of beta-proteins. The new function reveals new features in beta-protein folding: larger residues slow down the folding while alternative distribution of polar-non-polar residues accelerates the folding.

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Amino Acid Sequence Mathematics Protein Conformation Protein Folding Protein Structure, Secondary Proteins Journal Article Research Support, Non-U.S. Gov't

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Hui Shao, Zong-Hao Zeng. 2003. A sequence function reveals new features in beta-protein folding.. https://doi.org/10.2174/0929866033478690

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