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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Nmr Studies Of The Prionogenic Peptide Derived From Sup35 Protein

Author(s): Young Kee Chae, Kyunghee Lee and Yongae Kim

Volume 11 , Issue 1 , 2004

Page: [23 - 28] Pages: 6

DOI: 10.2174/0929866043478446

Price: $65

Abstract

The NMR studies of the prionogenic peptide derived from Sup35 are presented. The peptide molecules were dissolved in the half-aqueous solution to prevent severe aggregation, and were found to be in an extended conformation from the chemical shift and the coupling constant data. They could form higher order multimers by making intermolecular hydrogen bonds, judging from the observation that the NMR sample became a gel-like state at lower temperatures. This work reports the first structural information in the solution state about the prionogenic peptide mimicking the state of amyloid fibrils, and provides a solid foundation for further structural analysis of peptide molecules forming insoluble aggregates.

Keywords: Prionogenic Peptide, hydrogen bonds, NMR sample


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