Publisher: Bentham Science Publishers
E-ISSN: 1875-5305|10|5|435-439
ISSN: 0929-8665
Source: Protein and Peptide Letters, Vol.10, Iss.5, 2003-10, pp. : 435-439
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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 &bgr;-proteins. The new function reveals new features in &bgr;-protein folding: larger residues slow down the folding while alternative distribution of polar-non-polar residues accelerates the folding.
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