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A Minimal Protein Folding Model To Measure Hydrophobic and CH–π Effects on Interactions between Nonpolar Surfaces in Water
Author(s) -
Bhayana Brijesh,
Wilcox Craig S.
Publication year - 2007
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200700932
Subject(s) - folding (dsp implementation) , chemistry , measure (data warehouse) , protein folding , hydrophobic effect , chemical physics , molecule , biological system , computer science , data mining , organic chemistry , biochemistry , electrical engineering , engineering , biology
In the balance : A synthetic molecule that exhibits two‐state folding behavior in water is described. Quantitative experiments reveal that the microscopic hydrophobic effect is similar in magnitude to the CH–π interaction. These forces may therefore be equally important in the folding of aromatic‐rich regions of proteins. The method allows a new approach to the direct measurement of excess surface energy associated with nonpolar surfaces.