Structural Characterization of Backbone-Expanded Helices in Hybrid Peptides: (αγ)n and (αβ)n Sequences with Unconstrained β and γ Homologues of L-Val

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). C12 helices were observed in the αγ peptide series for n=2–8. In comparison, th...

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Published in:Angewandte Chemie International Edition 2012-08, Vol.51 (35), p.8736-8739
Main Authors: Basuroy, Krishnayan, Dinesh, Bhimareddy, Shamala, Narayanaswamy, Balaram, Padmanabhan
Format: Article
Language:English
Subjects:
backbone conformations
Crystallography, X-Ray
helices
hybrid peptides
Hydrogen Bonding
hydrogen bonds
Peptides - chemistry
Peptides - metabolism
Protein Structure, Secondary
Valine - chemistry
X-ray diffraction
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Summary: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). C12 helices were observed in the αγ peptide series for n=2–8. In comparison, the αα peptide and αβ peptide sequences show C10 and mixed C14/C15 helices, respectively.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201204436