The ability of α,β2,3-hybrid peptides with a heterochiral backbone to exist in a helical, extended, or partially folded state depending on the solvation conditions employed was investigated. The preference was found to be directly dictated by Cα-Cβ torsions in the β-residues. α,β-Hybrid peptides with a heterochiral backbone show the ability to exist in a helical, extended, or partially folded conformation depending on the solvation conditions employed. Copyright © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Kannoth Manheri Muraleedharan

Department Of Chemistry

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IIT Madras has been ranked as the top engineering institute in India for four years in a row by the National Institutional Ranking Framework of the MHRD

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IIT Madras

European Journal of Organic Chemistry

Unfolding of helical trans-β2,3-hybrid peptides with (α-β)nα composition, when executed by increasing solvent polarity or temperature, proceeded in a systematic manner with the turns unwinding sequentially; C-terminal region of these peptides were first to unwind and the process propagated towards N terminus with more and more β residues equilibrating from the gauche to the anti rotameric state across Cα£Cβ. This is evidenced by clear change in their CβH signal splitting, 3JCαH-CβH values, and sequential disappearance of i,i+2 NOEs. Helix-strand hybrid: Unfolding of helical trans-β2,3-hybrid peptides with (α-β)nα composition when executed by increasing solvent polarity or temperature, proceeded in a systematic manner with the turns unwinding sequentially; the C-terminal region of these peptides were first to unwind and the process propagated towards the N terminus with more and more β residues equilibrating from gauche to anti rotameric states across Cα£Cβ. © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Chemistry - A European Journal

Can Helical Peptides Unwind One Turn at a Time? - Controlled Conformational Transitions in α,β2,3-Hybrid Peptides

Anti or gauche? trans-β2,3-Amino acid residues that are known to promote extended structures in their peptides show specific rotamer preferences in response to an intramolecular hydrogen-bonding possibility, which facilitates the 11-helical structures in their 1:1 α,β-hybrid peptides (see figure). Preferences for the gauche conformation for all internal β residues and anti for the C-terminal residue in these peptides were confirmed by NMR spectroscopic and X-ray diffraction experiments. Copyright © 2012 WILEY-VCH Verlag GmbH &amp; Co. KGaA, Weinheim.

Journal	Data powered by TypesetEuropean Journal of Organic Chemistry
Publisher	Data powered by TypesetWiley-VCH Verlag
ISSN	1434193X
Open Access	No