Repeating Aspartic Acid Residues Prefer Turn-like Conformations in the Unfolded State: Implications for Early Protein Folding
Author:
Affiliation:
1. Deparment of Chemistry, Drexel University, Philadelphia, Pennsylvania 19026, United States
2. Institut für Organische Chemie und Chemische Biologie, Johann Wolfgang Goethe Universität, Max von Laue Strasse 7, 60438 Frankfurt, Germany
Funder
National Natural Science Foundation of China
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.1c06472
Reference64 articles.
1. A revised set of potentials for β-turn formation in proteins
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3. Stereochemistry of polypeptide chain configurations
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5. Peptide conformation and protein folding
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