Effect of Hydrophobic Interactions on the Folding Mechanism of β-Hairpins
Author:
Affiliation:
1. Biophysical Chemistry, Department of Chemistry, University of Konstanz, 78457 Konstanz, Germany
2. Department of Chemistry, University of Illinois at Chicago, 845 West Taylor Street, Chicago, Illinois 60607-7061, United States
Funder
Division of Chemistry
Alexander von Humboldt-Stiftung
Deutsche Forschungsgemeinschaft
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/jp506658x
Reference20 articles.
1. Tryptophan zippers: Stable, monomeric β-hairpins
2. Correction: Proc. Natl. Acad. Sci. U.S.A. 2002, 5599, 9081–9082.
3. Tryptophan Side Chain Electrostatic Interactions Determine Edge-to-Face vs Parallel-Displaced Tryptophan Side Chain Geometries in the Designed β-Hairpin “trpzip2”
4. Role of different β-turns in β-hairpin conformation and stability studied by optical spectroscopy
5. Residual Native Structure in a Thermally Denatured β-Hairpin
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