Unconstrained Homooligomeric gamma-Peptides Show High Propensity for C-14 Helix Formation

Basuroy, Krishnayan and Dinesh, Bhimareddy and Reddy, Madhusudana MB and Chandrappa, Siddapa and Raghothama, Srinivasarao and Shamala, Narayanaswamy and Balaram, Padmanabhan (2013) Unconstrained Homooligomeric gamma-Peptides Show High Propensity for C-14 Helix Formation. In: ORGANIC LETTERS, 15 (18). pp. 4866-4869.

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Abstract

Monosubstituted gamma(4)-residues (gamma(4)Leu, gamma(4)Ile, and gamma(4)Val) form helices even in short homooligomeric sequences. C-14 helix formation is established by X-ray diffraction in homooligomeric (gamma)(n) tetra-, hexa- and decapeptide sequences demonstrating the high propensity of gamma residues, with proteinogenic side chains, to adopt locally folded conformations.

Item Type:	Journal Article
Publication:	ORGANIC LETTERS
Publisher:	AMER CHEMICAL SOC
Additional Information:	Copyright for this article belongs to the AMER CHEMICAL SOC, USA
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit Division of Chemical Sciences > Sophisticated Instruments Facility (Continued as NMR Research Centre) Division of Physical & Mathematical Sciences > Physics
Date Deposited:	26 Feb 2014 07:32
Last Modified:	26 Feb 2014 07:33
URI:	http://eprints.iisc.ac.in/id/eprint/48474

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