Trifluoroethanol-Induced β → α Transition in β-Lactoglobulin: Hydration and Cosolvent Binding Studied by 2H, 17O, and 19F Magnetic Relaxation Dispersion
Author:
Affiliation:
1. Department of Biophysical Chemistry, Lund University, SE-22100 Lund, Sweden
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi035330l
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1. Conformational aspects of polypeptides. XI. The nitroaromatic effect
2. High Helical Propensity of the Peptide Fragments Derived from β-Lactoglobulin, a Predominantly β-sheet Protein
3. Mechanism of Stabilization of Helical Conformations of Polypeptides by Water Containing Trifluoroethanol
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