Premium
Structural Characterization of Backbone‐Expanded Helices in Hybrid Peptides: (αγ) n and (αβ) n Sequences with Unconstrained β and γ Homologues of L ‐Val
Author(s) -
Basuroy Krishnayan,
Dinesh Bhimareddy,
Shamala Narayanaswamy,
Balaram Padmanabhan
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201204436
Subject(s) - peptide , characterization (materials science) , chemistry , hydrogen bond , crystallography , stereochemistry , computer science , molecule , nanotechnology , biochemistry , materials science , organic chemistry
Learning your αβγ′s : The diversity of hydrogen‐bonding patterns in backbone‐expanded hybrid helices is shown by crystal‐structure determination of several oligomeric peptides (see scheme; C=gray; H=white; O=red; N=blue). C 12 helices were observed in the αγ peptide series for n =2–8. In comparison, the αα peptide and αβ peptide sequences show C 10 and mixed C 14 /C 15 helices, respectively.