A Simple Parameter Relating Sequences with Folding Rates of Small α Helical Proteins
It is found that the helix parameter (HP), which favors clustering of non-polar residues, is linearly correlated with the logarithms of rate constants of folding of small two-state α-helical proteins. The definition is HP = NH-1 Σ [fi+ (fi-1+fi+1) / 2], where fi=1 or -1, if the i'th residue is hydrophobic or hydrophilic, respectively, NH is the number of hydrophobic residues and the summation is taken over the hydrophobic residues.
Keywords: helical proteins; helix parameter; non-polar residues; two-state helical proteins
Document Type: Review Article
Publication date: 01 June 2003
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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