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