Minimal Protein Folding Model To Measure Hydrophobic and CH-π Effects on Interactions between Nonpolar Surfaces in Water

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‐ric...

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Veröffentlicht in:	Angewandte Chemie (International ed.) 2007-01, Vol.46 (36), p.6833-6836
Hauptverfasser:	Bhayana, Brijesh, Wilcox, Craig S
Format:	Artikel
Sprache:	eng
Schlagworte:	conformation analysis Gibbs energy hydrophobic interactions Models, Molecular Protein Folding solvent effects Thermodynamics Water - chemistry
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creator	Bhayana, Brijesh Wilcox, Craig S
description	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.
doi_str_mv	10.1002/anie.200700932
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subjects	conformation analysis Gibbs energy hydrophobic interactions Models, Molecular Protein Folding solvent effects Thermodynamics Water - chemistry
title	Minimal Protein Folding Model To Measure Hydrophobic and CH-π Effects on Interactions between Nonpolar Surfaces in Water
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