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 Acidsjournal_title
Amino acidsauthors
Huang JT,Xing DJ,Huang Wdoi
10.1007/s00726-011-1189-3subject
Has Abstractpub_date
2012-08-01 00:00:00pages
567-72issue
2eissn
0939-4451issn
1438-2199journal_volume
43pub_type
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