Influence of the C‐terminal substituent on the crystal‐state conformation of Adm peptides
Author:
Affiliation:
1. Département de ChimieUniversité de Montréal Montréal Québec Canada
2. Institute of Biomolecular ChemistryPadova Unit Padova Italy
3. Department of ChemistryUniversity of Padova Padova Italy
Funder
Centre in Green Chemistry and Catalysis
Natural Sciences and Engineering Research Council of Canada
Université de Montréal
Publisher
Wiley
Subject
Organic Chemistry,Biomaterials,Biochemistry,Biophysics
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/pep2.24121
Reference55 articles.
1. The 310helical conformation of a pentapeptide containing α-aminoisobutyric acid (Aib): X-ray crystal structure of Tos–(Aib)5–OMe
2. Linear oligopeptides. 81. Solid-state and solution conformation of homooligo(.alpha.-aminoisobutyric acids) from tripeptide to pentapeptide: evidence for a 310 helix
3. Structures of polypeptides from α-amino acids disubstituted at the α-carbon
4. Controls exerted by the Aib residue: Helix formation and helix reversal This article is a US Government work and, as such, is in the public domain in the United States of America.
5. The crystal structure of Z-(Aib)10 -OH at 0.65 Å resolution: three complete turns of 310 -helix
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