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Unprecedented Torsional Preferences in trans ‐β 2,3 ‐Amino Acid Residues and Formation of 11‐Helices in α,β 2,3 ‐Hybrid Peptides
Author(s) -
Balamurugan Dhayalan,
Muraleedharan Kannoth M.
Publication year - 2012
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201201415
Subject(s) - intramolecular force , residue (chemistry) , conformational isomerism , chemistry , amino acid residue , stereochemistry , hydrogen bond , amino acid , crystallography , peptide sequence , molecule , biochemistry , organic chemistry , gene
Anti or gauche ? trans ‐β 2,3 ‐Amino acid residues that are known to promote extended structures in their peptides show specific rotamer preferences in response to an intramolecular hydrogen‐bonding possibility, which facilitates the 11‐helical structures in their 1:1 α,β‐hybrid peptides (see figure). Preferences for the gauche conformation for all internal β residues and anti for the C‐terminal residue in these peptides were confirmed by NMR spectroscopic and X‐ray diffraction experiments.