Structural characterization of backbone-expanded helices in hybrid peptides: (αγ) n and (αβ) n sequences with unconstrained β and γ homologues of L-Val


Autoria(s): Basuroy, Krishnayan; Dinesh, Bhimareddy; Shamala, Narayanaswamy; Balaram, Padmanabhan
Data(s)

2012

Resumo

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. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Formato

application/pdf

Identificador

http://eprints.iisc.ernet.in/45047/1/ang_che_51-35_8736_2012.pdf

Basuroy, Krishnayan and Dinesh, Bhimareddy and Shamala, Narayanaswamy and Balaram, Padmanabhan (2012) Structural characterization of backbone-expanded helices in hybrid peptides: (αγ) n and (αβ) n sequences with unconstrained β and γ homologues of L-Val. In: Angewandte Chemie - International Edition, 51 (35). pp. 8736-8739.

Publicador

John Wiley & Sons

Relação

http://dx.doi.org/10.1002/anie.201204436

http://eprints.iisc.ernet.in/45047/

Palavras-Chave #Molecular Biophysics Unit #Physics
Tipo

Journal Article

PeerReviewed