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

Monosubstituted γ4-residues (γ4Leu, γ4Ile, and γ4Val) 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...

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Bibliographic Details
Published in:Organic letters 2013-09, Vol.15 (18), p.4866-4869
Main Authors: Basuroy, Krishnayan, Dinesh, Bhimareddy, Reddy, M. B. Madhusudana, Chandrappa, Siddapa, Raghothama, Srinivasarao, Shamala, Narayanaswamy, Balaram, Padmanabhan
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Crystallography, X-Ray
Models, Molecular
Molecular Structure
Peptides - chemical synthesis
Peptides - chemistry
Protein Conformation
Protein Structure, Secondary
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Summary:Monosubstituted γ4-residues (γ4Leu, γ4Ile, and γ4Val) 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.
ISSN:1523-7060
1523-7052
DOI:10.1021/ol402248s