Relationship between protein folding kinetics and amino acid properties.

Abstract:

:The successful prediction of protein-folding rates based on the sequence-predicted secondary structure suggests that the folding rates might be predicted from sequence alone. To pursue this question, we directly predict the folding rates from amino acid sequences, which do not require any information on secondary or tertiary structure. Our work achieves 88% correlation with folding rates determined experimentally for proteins of all folding types and peptide, suggesting that almost all of the information needed to specify a protein's folding kinetics and mechanism is comprised within its amino acid sequence. The influence of residue on folding rate is related to amino acid properties. Hydrophobic character of amino acids may be an important determinant of folding kinetics, whereas other properties, size, flexibility, polarity and isoelectric point, of amino acids have contributed little to the folding rate constant.

journal_name

Amino Acids

journal_title

Amino acids

authors

Huang JT,Xing DJ,Huang W

doi

10.1007/s00726-011-1189-3

subject

Has Abstract

pub_date

2012-08-01 00:00:00

pages

567-72

issue

2

eissn

0939-4451

issn

1438-2199

journal_volume

43

pub_type

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