How the folding rates of two- and multistate proteins depend on the amino acid properties
Corresponding Author
Jitao T. Huang
Department of Chemistry and State Key Laboratory of EOC, College of Chemistry, Nankai University, Tianjin, 300071 China
Correspondence to: Jitao T. Huang, Department of Chemistry and State Key Laboratory of EOC, College of Chemistry, Nankai University, Tianjin 300071, China. E-mail: [email protected]Search for more papers by this authorWei Huang
Department of Chemistry and State Key Laboratory of EOC, College of Chemistry, Nankai University, Tianjin, 300071 China
Search for more papers by this authorShanran R. Huang
Department of Chemistry and State Key Laboratory of EOC, College of Chemistry, Nankai University, Tianjin, 300071 China
Search for more papers by this authorXin Li
Department of Chemistry and State Key Laboratory of EOC, College of Chemistry, Nankai University, Tianjin, 300071 China
Search for more papers by this authorCorresponding Author
Jitao T. Huang
Department of Chemistry and State Key Laboratory of EOC, College of Chemistry, Nankai University, Tianjin, 300071 China
Correspondence to: Jitao T. Huang, Department of Chemistry and State Key Laboratory of EOC, College of Chemistry, Nankai University, Tianjin 300071, China. E-mail: [email protected]Search for more papers by this authorWei Huang
Department of Chemistry and State Key Laboratory of EOC, College of Chemistry, Nankai University, Tianjin, 300071 China
Search for more papers by this authorShanran R. Huang
Department of Chemistry and State Key Laboratory of EOC, College of Chemistry, Nankai University, Tianjin, 300071 China
Search for more papers by this authorXin Li
Department of Chemistry and State Key Laboratory of EOC, College of Chemistry, Nankai University, Tianjin, 300071 China
Search for more papers by this authorABSTRACT
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.
Supporting Information
Additional Supporting Information may be found in the online version of this article.
| Filename | Description |
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| prot24599-sup-0001-supptable1.pdf223.7 KB | Supplementary Information Table 1. |
| prot24599-sup-0002-supptable2.pdf195.9 KB | Supplementary Information Table 2. |
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