Unconstrained Homooligomeric gamma-Peptides Show High Propensity for C-14 Helix Formation
| Data(s) |
2013
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|---|---|
| Resumo |
Monosubstituted gamma(4)-residues (gamma(4)Leu, gamma(4)Ile, and gamma(4)Val) form helices even in short homooligomeric sequences. C-14 helix formation is established by X-ray diffraction in homooligomeric (gamma)(n) tetra-, hexa- and decapeptide sequences demonstrating the high propensity of gamma residues, with proteinogenic side chains, to adopt locally folded conformations. |
| Formato |
application/pdf |
| Identificador |
http://eprints.iisc.ernet.in/48474/1/Org_Let_15-18_4866_2013.pdf Basuroy, Krishnayan and Dinesh, Bhimareddy and Reddy, Madhusudana MB and Chandrappa, Siddapa and Raghothama, Srinivasarao and Shamala, Narayanaswamy and Balaram, Padmanabhan (2013) Unconstrained Homooligomeric gamma-Peptides Show High Propensity for C-14 Helix Formation. In: ORGANIC LETTERS, 15 (18). pp. 4866-4869. |
| Publicador |
AMER CHEMICAL SOC |
| Relação |
http://dx.doi.org/10.1021/ol402248s http://eprints.iisc.ernet.in/48474/ |
| Palavras-Chave | #Molecular Biophysics Unit #Sophisticated Instruments Facility #Physics |
| Tipo |
Journal Article PeerReviewed |
