Sonti, Rajesh ; Dinesh, Bhimareddy ; Basuroy, Krishnayan ; Raghothama, Srinivasarao ; Shamala, Narayanaswamy ; Balaram, Padmanabhan (2014) C12 Helices in Long Hybrid (αγ)n Peptides Composed Entirely of Unconstrained Residues with Proteinogenic Side Chains Organic Letters, 16 (6). pp. 1656-1659. ISSN 1523-7060
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Official URL: http://doi.org/10.1021/Ol500307P
Related URL: http://dx.doi.org/10.1021/Ol500307P
Abstract
Unconstrained γ(4) amino acid residues derived by homologation of proteinogenic amino acids facilitate helical folding in hybrid (αγ)n sequences. The C12 helical conformation for the decapeptide, Boc-[Leu-γ(4)(R)Val]5-OMe, is established in crystals by X-ray diffraction. A regular C12 helix is demonstrated by NMR studies of the 18 residue peptide, Boc-[Leu-γ(4)(R)Val]9-OMe, and a designed 16 residue (αγ)n peptide, incorporating variable side chains. Unconstrained (αγ)n peptides show an unexpectedly high propensity for helical folding in long polypeptide sequences.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to American Chemical Society. |
| ID Code: | 131242 |
| Deposited On: | 06 Dec 2022 05:32 |
| Last Modified: | 30 Jan 2023 10:32 |
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