Chandrasekhar, K. ; Das, Manoj K. ; Anil Kumar, ; Balaram, P. (1988) Molecular conformation of alamethicin in dimethylsulfoxide solution. A two-dimensional n.m.r. study International Journal of Peptide and Protein Research, 32 (3). pp. 167-174. ISSN 0367-8377
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Official URL: http://www3.interscience.wiley.com/journal/1216348...
Related URL: http://dx.doi.org/10.1111/j.1399-3011.1988.tb00931.x
Abstract
The solution conformation of alamethicin, a 20-residue antibiotic peptide, has been investigated using two-dimensional n.m.r. spectroscopy. Complete proton resonance assignments of this peptide have been carried out using COSY, SUPERCOSY, RELAY COSY and NOESY two-dimensional spectroscopies. Observation of a large number of nuclear Overhauser effects between sequential backbone amide protons, between backbone amide protons and CβH protons of preceding residues and extensive intramolecular hydrogen bonding patterns of NH protons has established that this polypeptide is in a largely helical conformation. This result is in conformity with earlier reported solid state X-ray results and a recent n.m.r. study in methanol solution (Esposito et al. (1987) Biochemistry26, 1043-1050) but is at variance with an earlier study which favored an extended conformation for the C-terminal half of alamethicin (Bannerjee et al. (1983) J. Mol. Biol.165, 757-775).
Item Type: | Article |
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Source: | Copyright of this article belongs to Munksgaard International Publishers. |
Keywords: | Alamethicin; N.M.R; Peptide Conformation |
ID Code: | 4452 |
Deposited On: | 18 Oct 2010 07:50 |
Last Modified: | 16 May 2016 15:06 |
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