A Sequence Function Reveals New Features In β-Protein Folding

Hui      Shao; Zong-Hao      Zeng

doi:10.2174/0929866033478690

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 β-proteins. The new function reveals new features in β-protein folding: larger residues slow down the folding while alternative distribution of polar-non-polar residues accelerates the folding.

Keywords: Protein, polar-non-polar residues

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Protein & Peptide Letters

Title: A Sequence Function Reveals New Features In β-Protein Folding

Volume: 10 Issue: 5

Author(s): Hui Shao and Zong-Hao Zeng

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Keywords: Protein, polar-non-polar residues

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 β-proteins. The new function reveals new features in β-protein folding: larger residues slow down the folding while alternative distribution of polar-non-polar residues accelerates the folding.

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Shao Hui and Zeng Zong-Hao, A Sequence Function Reveals New Features In β-Protein Folding, Protein & Peptide Letters 2003; 10 (5) . https://dx.doi.org/10.2174/0929866033478690