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

Basuroy Krishnayan | Zendy; Dinesh Bhimareddy | Zendy; Shamala Narayanaswamy | Zendy; Balaram Padmanabhan | Zendy

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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.

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