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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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Official URL: http://dx.doi.org/10.1021/ol402248s


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
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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