An Enhanced β Turn in Water
Author:
Affiliation:
1. Center for Advanced Drug Research (CADRE), SRI International, 140 Research Drive, Harrisonburg, Virginia 22802, United States
Publisher
American Chemical Society (ACS)
Subject
Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/ol2024983
Reference22 articles.
1. Studies of folded peptide-based catalysts for asymmetric organic synthesis
2. Role of Local Sequence in the Folding of Cellular Retinoic Acid Binding Protein I: Structural Propensities of Reverse Turns
3. Design of Short Linear Peptides That Show Hydrogen Bonding Constraints in Water
4. Determinants of fold stabilizing aromatic-aromatic interactions in short peptides
5. A conformational study of peptides with the general structure Ac-L-Xaa-Pro-D-Xaa-L-Xaa-NH2: spectroscopic evidence for a peptide with significant .beta.-turn character in water and in dimethyl sulfoxide
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