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• W2000123367 abstract "phi(f)-value analysis is one of the most common methods to characterize the structure of protein folding transition states. It compares the effects of mutations on the folding kinetics with the respective effects on equilibrium stability. The interpretation of the results usually focuses on a few unusual phi(f)-values, which are either particularly high or which are larger than 1 or smaller than 0. These mutations are believed to affect the most important regions for the folding process. A major uncertainty in experimental phi(f)-values is introduced by the commonly used analysis of only a single mutant at various positions in a protein (two-point analysis). To test the reliability of two-point phi(f)-values we used reference data from three positions in two different proteins at which multiple mutations have been introduced. The results show that two-point phi(f)-values are highly inaccurate if the difference in stability between two variants is less than 7 kJ/mol, corresponding to a 20-fold difference in equilibrium constant. Comparison with reported phi(f)-values for 11 proteins shows that most unusual phi(f)-values are observed in mutants which show changes in protein stability that are too small to allow a reliable analysis. The results argue against specific nucleation sites in protein folding and give a picture of transition states as distorted native states for the major part of a protein or for large substructures." @default.
• W2000123367 created "2016-06-24" @default.
• W2000123367 creator A5022329235 @default.
• W2000123367 creator A5027755462 @default.
• W2000123367 date "2003-12-01" @default.
• W2000123367 modified "2023-10-16" @default.
• W2000123367 title "Origin of Unusual φ-values in Protein Folding: Evidence Against Specific Nucleation Sites" @default.
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• W2000123367 doi "https://doi.org/10.1016/j.jmb.2003.10.016" @default.
• W2000123367 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/14643667" @default.
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