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
PDF
893kB |
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 |
Repository Staff Only: item control page