C-12 Helices in Long Hybrid (alpha gamma)(n) Peptides Composed Entirely of Unconstrained Residues with Proteinogenic Side Chains

Sonti, Rajesh and Dinesh, Bhimareddy and Basuroy, Krishnayan and Raghothama, Srinivasarao and Shamala, Narayanaswamy and Balaram, Padmanabhan (2014) C-12 Helices in Long Hybrid (alpha gamma)(n) Peptides Composed Entirely of Unconstrained Residues with Proteinogenic Side Chains. In: ORGANIC LETTERS, 16 (6). pp. 1656-1659.

PDF org_let_16-6_1656_2014.pdf - Published Version Restricted to Registered users only Download (4MB) | Request a copy

Abstract

Unconstrained gamma(4) amino acid residues derived by homologation of proteinogenic amino acids facilitate helical folding in hybrid (alpha gamma)(n) sequences. The C-12 helical conformation for the decapeptide, Boc-Leu-gamma(4)(R)Val](5)-OMe, is established in crystals by X-ray diffraction. A regular C-12 helix is demonstrated by NMR studies of the 18 residue peptide, Boc-Leu-gamma(4)(AR)Val](9)-OMe, and a designed 16 residue (alpha gamma)(n) peptide, incorporating variable side chains. Unconstrained (alpha gamma)(n) peptides show an unexpectedly high propensity for helical folding in long polypeptide sequences.

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 > NMR Research Centre (Formerly Sophisticated Instruments Facility) Division of Physical & Mathematical Sciences > Physics
Date Deposited:	15 May 2014 10:38
Last Modified:	15 May 2014 10:38
URI:	http://eprints.iisc.ac.in/id/eprint/49038

Actions (login required)

View Item