Folding and Unfolding of the Tryptophan Zipper in the Presence of Two Thioamide Substitutions
Author:
Affiliation:
1. Department of Chemistry, University of Zurich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland
Funder
Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
Universität Zürich
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/acs.jpcb.1c03327
Reference44 articles.
1. Two-dimensional infrared measurements of the coupling between amide modes of an α-helix
2. Parallel β-Sheet Vibrational Couplings Revealed by 2D IR Spectroscopy of an Isotopically Labeled Macrocycle: Quantitative Benchmark for the Interpretation of Amyloid and Protein Infrared Spectra
3. -Helix folding in the presence of structural constraints
4. Site-Specific Relaxation Kinetics of a Tryptophan Zipper Hairpin Peptide Using Temperature-Jump IR Spectroscopy and Isotopic Labeling
5. Broad-Band Ultraviolet CD Spectroscopy of Ultrafast Peptide Backbone Conformational Dynamics
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