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Nmr Studies Of The Prionogenic Peptide Derived From Sup35 Protein

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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.
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Keywords: NMR sample; Prionogenic Peptide; hydrogen bonds

Document Type: Review Article

Affiliations: Department of Applied Chemistry and Recombinant Protein Expression Center (RPEC), Sejong University, 98 Gunja-Dong, Gwangjin-Gu, Seoul, Korea, 143-747,

Publication date: 01 February 2004

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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