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Amino Acid Sequence Predicts Folding Rate for Middle‐size Two‐state Proteins by Ji‐Tao Huang; Jing Tian is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
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## Abstract The significant correlation between protein folding rates and the sequence‐predicted secondary structure suggests that folding rates are largely determined by the amino acid sequence. Here, we present a method for predicting the folding rates of proteins from sequences using the intrinsic properties of amino acids, which does not require any information on secondary structure prediction and structural topology. The contribution of residue to the folding rate is expressed by the residue's Ω value. For a given residue, its Ω depends on the amino acid properties (amino acid rigidity and dislike of amino acid for secondary structures). Our investigation achieves 82% correlation with folding rates determined experimentally for simple, two‐state proteins studied until the present, suggesting that the amino acid sequence of a protein is an important determinant of the protein‐folding rate and mechanism. Proteins 2006. © 2006 Wiley‐Liss, Inc.
Who reads Amino Acid Sequence Predicts Folding Rate for Middle‐size Two‐state Proteins?
It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- Ji‐Tao Huang; Jing Tian
- Publisher
- John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Liss Inc; Wiley (ISSN 0887-3585)
- Published
- 2006
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)