Premium
How the folding rates of two‐ and multistate proteins depend on the amino acid properties
Author(s) -
Huang Jitao T.,
Huang Wei,
Huang Shanran R.,
Li Xin
Publication year - 2014
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24599
Subject(s) - chemistry , amino acid , phi value analysis , lattice protein , protein folding , folding (dsp implementation) , cysteine , amino acid residue , folding funnel , kinetics , biophysics , isoelectric point , contact order , native state , downhill folding , crystallography , biochemistry , peptide sequence , biology , physics , quantum mechanics , electrical engineering , gene , enzyme , engineering
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. Proteins 2014; 82:2375–2382. © 2014 Wiley Periodicals, Inc.