Unconstrained Homooligomeric γ-Peptides Show High Propensity for C14 Helix Formation

Basuroy, Krishnayan ; Dinesh, Bhimareddy ; Reddy, M. B. Madhusudana ; Chandrappa, Siddapa ; Raghothama, Srinivasarao ; Shamala, Narayanaswamy ; Balaram, Padmanabhan (2013) Unconstrained Homooligomeric γ-Peptides Show High Propensity for C14 Helix Formation Organic Letters, 15 (18). pp. 4866-4869. ISSN 1523-7060

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Official URL: http://doi.org/10.1021/Ol402248S

Related URL: http://dx.doi.org/10.1021/Ol402248S

Abstract

Monosubstituted γ(4)-residues (γ(4)Leu, γ(4)Ile, and γ(4)Val) form helices even in short homooligomeric sequences. C14 helix formation is established by X-ray diffraction in homooligomeric (γ)n tetra-, hexa- and decapeptide sequences demonstrating the high propensity of γ residues, with proteinogenic side chains, to adopt locally folded conformations.

Item Type:Article
Source:Copyright of this article belongs to American Chemical Society.
ID Code:131239
Deposited On:06 Dec 2022 05:14
Last Modified:30 Jan 2023 10:42

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