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Hydrophobic channels in crystals of an alpha-aminoisobutyric acid pentapeptide

Rao, Ch Pulla and Shamala, N and Nagaraj, R and Rao, CNR and Balaram, P (1981) Hydrophobic channels in crystals of an alpha-aminoisobutyric acid pentapeptide. In: Biochemical and Biophysical Research Communications, 103 (3). pp. 898-904.

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The crystal structure of the pentapeptide p-toluene-sulfonyl-(α-aminoisobutyryl)5-methyl ester (Tosyl-(Aib)5-OMe) has been determined in the space group PImage . Pentapeptide molecules are folded in the 310 helical conformation and packed together, so as to yield a hydrophobic channel with a minimim diameter of 5.2 �. The channel contains crystallographically disordered material. This structure provides a model for channel formation by hydrophobic peptide aggregates and should prove useful in studies of alamethicin, suzukacillin and related Aib containing membrane channels. Triclinic (PImage ) crystals of the pentapeptide are obtained in the presence of LiClO4 in aqueous methanol, whereas crystallization from methanol alone yields crystals in the space group Pbca. The conformations of the peptide in the two crystal forms are very similar and only the molecular packing is dramatically different.

Item Type: Journal Article
Publication: Biochemical and Biophysical Research Communications
Publisher: Elsevier Science
Additional Information: Copyright of this article belongs to Elsevier Science.
Department/Centre: Division of Chemical Sciences > Solid State & Structural Chemistry Unit
Date Deposited: 31 Aug 2009 04:59
Last Modified: 19 Sep 2010 05:42
URI: http://eprints.iisc.ac.in/id/eprint/22658

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