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Membrane Channel Forming Polypeptides. 270-MHz Proton Magnetic Resonance Studies of the Aggregation of the 11-21 Fragment of Suzukacillin in Organic Solvents

Iqbal, M and Balaram, P (1981) Membrane Channel Forming Polypeptides. 270-MHz Proton Magnetic Resonance Studies of the Aggregation of the 11-21 Fragment of Suzukacillin in Organic Solvents. In: Biochemistry, 20 (25). pp. 7278-7284.

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Abstract

270-MHz 1H NMR studies of the 11-21 suzukacillin fragment Boc-Gln-Aib-Leu-Aib-Gly-Leu-Aib-Val-Aib-Aib-OMe (11-G) and its analogue Boc-Ala-Aib-Leu-Aib-Gly-Leu-Aib-Pro-Val-Aib-Aib-OMe (11-A) have been carried out in $CD{Cl}_3$ and ${({CD}_3)}_2SO$. The NH chemical shifts and their temperature coefficients have been measured as a function of peptide concentration in both solvents. It is established that replacement of Gln by Ala is without effect on backbone conformation. Both peptides adopt highly folded $3_{10}$ helical conformations stabilized by seven intramolecular 4 \rightarrow 1 hydrogen bonds. Nonlinear temperature dependences are demonstrated for free NH groups in the Gln(1) peptide. Aggregation is mediated by intermolecular hydrogen bonds formed by solvent-exposed NH groups. A major role for the Gln side chain in peptide association is suggested by differences in the NMR behavior of the Gln(1) and Ala(1) peptides. For the Gln(1) peptide in $CD{Cl}_3$, the carboxamide side chain carbonyl group forms an intramolecular hydrogen bond to the peptide backbone, while the trans side chain NH shows evidence for intermolecular interactions. In ${({CD}_3)}_2SO$, the cis carboxamide NH is involved in intermolecular hydrogen bonding. The possible role of the central Gln residue in sta-bilizing aggregates of peptide channel formers is discussed, and a model for hexameric association is postulated.

Item Type: Journal Article
Additional Information: Copyright for this article belongs to American Chemical Society.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Depositing User: M.K Anitha
Date Deposited: 01 Jun 2005
Last Modified: 19 Sep 2010 04:19
URI: http://eprints.iisc.ac.in/id/eprint/3264

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