title: How the folding rates of two- and multistate proteins depend on the amino acid properties.
abstract: Proteins fold by either two-state or multistate kinetic mechanism. We observe that amino acids play different roles in different mechanism. Many residues that are easy to form regular secondary structures (α helices, β sheets and turns) can promote the two-state folding reactions of small proteins. Most of hydrophilic residues can speed up the multistate folding reactions of large proteins. Folding rates of large proteins are equally responsive to the flexibility of partial amino acids. Other properties of amino acids (including volume, polarity, accessible surface, exposure degree, isoelectric point, and phase transfer energy) have contributed little to folding kinetics of the proteins. Cysteine is a special residue, it triggers two-state folding reaction and but inhibits multistate folding reaction. These findings not only provide a new insight into protein structure prediction, but also could be used to direct the point mutations that can change folding rate.
authors.affiliation: Department of Chemistry and State Key Laboratory of EOC, College of Chemistry, Nankai University, Tianjin, 300071, China.
authors.forename: Jitao T
authors.initials: JT
authors.lastname: Huang
authors.forename: Wei
authors.initials: W
authors.lastname: Huang
authors.forename: Shanran R
authors.initials: SR
authors.lastname: Huang
authors.forename: Xin
authors.initials: X
authors.lastname: Li
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D003627:Data Interpretation, Statistical; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D007526:Isoelectric Point; D007700:Kinetics; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
chemical_list: D000596:Amino Acids; D011506:Proteins
keywords: amino acid property; cysteine; flexibility; hydrophobicity; protein folding; secondary structural propensity