Nmr Studies Of The Prionogenic Peptide Derived From Sup35 Protein

Title: Nmr Studies Of The Prionogenic Peptide Derived From Sup35 Protein

Volume: 11 Issue: 1

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

Affiliation:

Keywords: Prionogenic Peptide, hydrogen bonds, NMR sample

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.

Cite this article as:

Chae Kee Young, Lee Kyunghee and Kim Yongae, Nmr Studies Of The Prionogenic Peptide Derived From Sup35 Protein, Protein & Peptide Letters 2004; 11 (1) . https://dx.doi.org/10.2174/0929866043478446