Chandrasekhar, K and Das, Manoj K and Kumar, Anil and Balaram, P (1988) Molecular conformation of alamethicin in dimethylsulfoxide solution A two-dimensional n.m.r. study. In: International Journal of Peptide & Protein Research, 32 (3). pp. 167-174.
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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.
| Item Type: | Journal Article |
|---|---|
| Publication: | International Journal of Peptide & Protein Research |
| Publisher: | John Wiley & Sons |
| Additional Information: | Copyright of this article belongs to John Wiley & Sons |
| Keywords: | Alamethicin;n.m.r.;peptide conformation. |
| Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit Division of Chemical Sciences > Sophisticated Instruments Facility (Continued as NMR Research Centre) Division of Physical & Mathematical Sciences > Physics |
| Date Deposited: | 23 Sep 2010 09:39 |
| Last Modified: | 23 Sep 2010 09:39 |
| URI: | http://eprints.iisc.ac.in/id/eprint/32389 |
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