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Diversity of the gramicidin a spatial structure: two-dimensional 1H nmr study in solution

✍ Scribed by V.F. Bystrov; A.S. Arseniev

Publisher
Elsevier Science
Year
1988
Tongue
French
Weight
999 KB
Volume
44
Category
Article
ISSN
0040-4020

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✦ Synopsis

Theoretical consideration reveals a unique relationship between NMR spectral parameters and possible types of the gramididin A spatial structure. By means of two dimensional NMR spectroscopy four distinct species were detected simultaneously in ethanol solution. Comparison of experimental data and theoretical conclusions demonstrates that species 1 and 2 are left-handed parallel double helices ttqq,~ 5 6 differina in relative arranaement of the two polypeptide chai&"within the-dimers, species 3 is left-handed antiparallel double helix +tlT5 6, and species 4 is a mirror imaqe of snecies I. i.e. riaht-hande Lg oarallel double helix ttgq&6. The results are compared with ihose on spatial structures of the peptide lex with cesium (right-handed antiparallel double helix ) and of the gramicidin A transmembrane ion-channel (N-termina to N-terminal single-stranded dimert 3 6.3 6.3). ID LD Gramicidin A (GA) is a linear pentadecapeptide, HCO-L-Val1-Gly2-L-Ala3-~-Leu4-L-Ala5-~-Va16-L-Va17-~-

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