title: 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.
authors.affiliation: State Key Laboratory of Elemento-Organic Chemistry, College of Chemistry, Nankai University, Tianjin 300071, China. jthuang@nankai.edu.cn
authors.forename: Jitao T
authors.initials: JT
authors.lastname: Huang
authors.forename: Dajie J
authors.initials: DJ
authors.lastname: Xing
authors.forename: Wei
authors.initials: W
authors.lastname: Huang
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids; D003198:Computer Simulation; D003627:Data Interpretation, Statistical; D057927:Hydrophobic and Hydrophilic Interactions; D007526:Isoelectric Point; D007700:Kinetics; D016014:Linear Models; D008958:Models, Molecular; D017510:Protein Folding; D017433:Protein Structure, Secondary
chemical_list: D000596:Amino Acids