The helical conformations of 14- and 16-residue fragments of suzukacillin, a membrane channel-forming polypeptide
Data(s) |
01/09/1982
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Resumo |
The suzukacillin fragments, Boc-Ala-Aib-Aib-Gln-Aib-Leu-Aib-Gly-Leu-Aib-Pro-Val-Aib-Aib-OMe (14), Boc-Ala-Aib-Ala-Aib-Aib-Gln-Aib-Leu-Aib-Gly-Leu-Aib-Pro-Val-Aib-Aib-OMe (16G) and the completely apolar 16-residue peptide in which the glutamine residue has been replaced by alanine (16A) have been studied by 270 MHz 1H-HMR, in C2HCl3 and (C2H3)2SO solution. Intramolecularly hydrogen-bonded NH groups have been identified by temperature and solvent dependence of chemical shifts. Peptides 14 and 16A adopt folded 310 helical conformations stabilized by 11 and 13 hydrogen bonds, respectively. In peptide 16G there are 12 intramolecular hydrogen bonds, with the glycine NH being solvent-exposed, in contrast to 14 and 16A. |
Formato |
application/pdf |
Identificador |
http://eprints.iisc.ernet.in/20908/1/fulltext.pdf Iqbal, M and Balaram, P (1982) The helical conformations of 14- and 16-residue fragments of suzukacillin, a membrane channel-forming polypeptide. In: Biochimica et Biophysica Acta (BBA), 706 (2). pp. 179-187. |
Publicador |
Elsevier Science |
Relação |
http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6T21-47RSD6C-15P&_user=512776&_rdoc=1&_fmt=&_orig=search&_sort=d&view=c&_acct=C000025298&_version=1&_urlVersion=0&_userid=512776&md5=1478c01f2a31eb607c9dc275eb5e5e95 http://eprints.iisc.ernet.in/20908/ |
Palavras-Chave | #Molecular Biophysics Unit |
Tipo |
Journal Article PeerReviewed |