Helical conformations of three crystalline pentapeptide fragments of suzukacillin, a membrane channel forming polypeptide


Autoria(s): Francis, AK; Rao, Ch Pulla; Iqbal, M; Nagaraj, R; Vijayan, M; Balaram, P
Data(s)

01/06/1982

Resumo

The crystal structures of three pentapeptide fragments of suzukacillin-A have been determined. Boc-Aib-Pro-Val-Aib-Val-OMe (peptide 1–5) adopts a distorted helical conformation, stabilized by three intramolecular hydrogen bonds (two 5→1, one 4→1). Boc-Ala-Aib-Ala-Aib-Aib-OMe (peptide 6–10) and Boc-Leu-Aib-Pro-Val-Aib-OMe (peptide 16–20) adopt 310 helical structures stabilized by three and two 4→1 intramolecular hydrogen bonds, respectively. These structures provide substantial support for a largely helical conformation for the suzukacillin membrane channel.

Formato

application/pdf

Identificador

http://eprints.iisc.ernet.in/21454/1/fulltext.pdf

Francis, AK and Rao, Ch Pulla and Iqbal, M and Nagaraj, R and Vijayan, M and Balaram, P (1982) Helical conformations of three crystalline pentapeptide fragments of suzukacillin, a membrane channel forming polypeptide. In: Biochemical and Biophysical Research Communications, 106 (4). pp. 1240-1247.

Publicador

Elsevier Science

Relação

http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6WBK-4DMX7GR-B8&_user=512776&_rdoc=1&_fmt=&_orig=search&_sort=d&_docanchor=&view=c&_acct=C000025298&_version=1&_urlVersion=0&_userid=512776&md5=bbc15665556e28ed3b616ac80303d4c2

http://eprints.iisc.ernet.in/21454/

Palavras-Chave #Solid State & Structural Chemistry Unit
Tipo

Journal Article

PeerReviewed