Pseudo-A(1,3) Strain as a Key Conformational Control Element in the Design of Poly-l-proline Type II Peptide Mimics
Author:
Affiliation:
1. Contribution from the Department of Chemistry, University of Vermont, Burlington, Vermont 05405
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja972494e
Reference22 articles.
1. The importance of extended conformations and, in particular, the PII conformation for the molecular recognition of peptides
2. Two Binding Orientations for Peptides to the Src SH3 Domain: Development of a General Model for SH3-Ligand Interactions
3. Structural basis for the binding of proline-rich peptides to SH3 domains
4. Structure of the p53 Tumor Suppressor Bound to the Ankyrin and SH3 Domains of 53BP2
5. Delineation of an Active Fragment and Poly(l-proline) II Conformation for Candidacidal Activity of Bactenecin 5
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