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Conserved nucleation sites reinforce the significance of Phi value analysis in protein‐folding studies
Author(s) -
Gianni Stefano,
Jemth Per
Publication year - 2014
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.1287
Subject(s) - protein folding , robustness (evolution) , folding (dsp implementation) , computational biology , mutagenesis , nucleation , value (mathematics) , statistical physics , chemistry , biology , computer science , bioinformatics , biological system , mathematics , physics , mutant , genetics , statistics , thermodynamics , biochemistry , engineering , electrical engineering , gene
The only experimental strategy to address the structure of folding transition states, the so‐called Φ value analysis, relies on the synergy between site directed mutagenesis and the measurement of reaction kinetics. Despite its importance, the Φ value analysis has been often criticized and its power to pinpoint structural information has been questioned. In this hypothesis, we demonstrate that comparing the Φ values between proteins not only allows highlighting the robustness of folding pathways but also provides per se a strong validation of the method. © 2014 IUBMB Life, 66(7):449–452, 2014
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