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Conformational analysis of sea cucumber (Caudina arenicola) C globin 94-97 fragment, Pro-Glu-Leu-Leu.

作者信息

Sunil Kumar P N, Devaky K S, Sadasivan C, Haridas M

机构信息

School of Biosciences, Mahatma Gandhi University, Kottayam-686 560, Kerala, India.

出版信息

Protein Pept Lett. 2002 Oct;9(5):403-9. doi: 10.2174/0929866023408526.

Abstract

The tetrapeptide Pro-Glu-Leu-Leu forms the 94-97 fragment of C globin in sea cucumber. 2% Butanediol dimethacrylate-cross linked polystyrene (2% BDDMA-PS), which had been optimized, was used for the synthesis of the tetrapeptide Pro-Glu-Leu-Leu. The peptide was synthesized by using Boc-amino acid strategy. The peptide purity was checked by RP-HPLC and the peptide was characterized by (1)H NMR spectroscopy and amino acid analysis. Conformation of the peptide was studied by 1D- and 2D- homonuclear (1)H NMR, in DMSO-d6 at 300K. The conformation of the synthetic tetrapeptide (extended backbone conformation) is not in agreement with that in C globin.

摘要

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