Hydrophobic channels in crystals of an α-aminoisobutyric acid pentapeptide

Pulla Rao, Ch. ; Shamala, N. ; Nagaraj, R. ; Rao, C. N. R. ; Balaram, P. (1981) Hydrophobic channels in crystals of an α-aminoisobutyric acid pentapeptide Biochemical and Biophysical Research Communications, 103 (3). pp. 898-904. ISSN 0006-291X

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/000629...

Related URL: http://dx.doi.org/10.1016/0006-291X(81)90895-0


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 PI . 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 Å. 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 (PI) 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.

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Deposited On:25 Nov 2010 13:13
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