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Crystal Structure of Boc-Ala-Aib-Ala-Aib-Aib-Methyl Ester, A Pentapeptide Fragment of the Channel-Forming Ionophore Suzukacillin

Francis, AK and Iqbal, M and Balaram, P and Vijayan, M (1983) Crystal Structure of Boc-Ala-Aib-Ala-Aib-Aib-Methyl Ester, A Pentapeptide Fragment of the Channel-Forming Ionophore Suzukacillin. In: Biopolymers, 22 (6). pp. 1499-1505.

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Abstract

t -Butyloxycarbonyl-L-alanyl-a-aminoisobutyryl-L-alanyl-\alpha-aminoisobutyryl-\alpha-aminoisobutyric acid methyl ester (t-Boc-L-Ala-Aib-L-Ala-Aib-Aib-OMe), $C_{24}H_{43}N_5O_8$, an end-protected pentapeptide with a sequence corresponding to the 6th through the 10th residues in suzukacillin, crystallizes in the orthorhombic space group ${P2}_12_12_1$ with a = 11.671, b = 14.534, c = 17.906 A,and z = 4. The molecule exists as a right-handed $3_{10}$-helix with a pitch of 6.026 A. The helix is stabilized by three 4 \rightarrow 1 hydrogen bonds with the NH groups of Ala(3), Aib(4), and Aib(5) hydrogen bonding to the carbonyl oxygens of t-Boc, Ala(1), and Aib(2), respectively. The helical molecules arrange themselves in a head-to-tail fashion along the a direction in such a way that the NH groups of Ala(1) and Aib(2) hydrogen bond to the carbonyl oxygens of Aib(4) and Aib(5), respectively, of a translationally related molecule. The helical columns thus formed close-pack nearly hexagonally to form the crystal.

Item Type: Journal Article
Additional Information: Copyright for this article belongs to John Wiley & Sons, Inc.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 15 Mar 2005
Last Modified: 19 Sep 2010 04:18
URI: http://eprints.iisc.ernet.in/id/eprint/2906

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