Determinação da estrutura terciária do peptídeo Cn-AMP1 isolado da água do coco verde, por Ressonância Magnética Nuclear (RMN)
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2013-03-12
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Universidade Federal de Goiás
Resumo
This study aims to determine and analyze the three-dimensional structure in the lowest energy conformation of the peptide Cn-AMP1, isolated from green coconut water by 1H NMR. The determination of the 3D structure of the peptide under study was performed by homonuclear 2D 1H NMR experiments COSY, TOCSY and NOESY, using a 1 mM solution of the peptide Cn-AMP1 on Bruker AVANCE III 500 MHz (for 1H). The analysis of the correlation maps were made using the software NMRView, and the methodology adopted was the allocation sequence described by Wüthrich, where 200 structures were generated and selected the 20 lowest energy conformations to represent the overall three-dimensional structure Cn-AMP1 peptide. The peptide showed helical structure between residues Ser-1and Ala-6 in SDS- d25 micelles, 100 mM being structured randomly between residues Gln-7 and Met-9. However, under conditions of physiological pH, as in the absence of SDS micelles d25, the peptide showed no helix structure, predominating is randomly.
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SANTANA, M. J. Determinação da estrutura terciária do peptídeo Cn-AMP1 isolado da água do coco verde, por Ressonância Magnética Nuclear (RMN). 2013. 104 f. Dissertação (Mestrado em Química) - Universidade Federal de Goiás, Goiânia, 2013.