NMR identification of left-handed polyproline type II helices
Author:
Publisher
Wiley
Subject
Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics
Reference61 articles.
1. Left-handed Polyproline II Helices Commonly Occur in Globular Proteins
2. Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase
3. Structural basis for the binding of proline-rich peptides to SH3 domains
4. High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides
5. Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains
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