NR AQZX
AU Chae,Y.K.; Lee,K.; Kim,Y.
TI NMR studies of the prionogenic peptide derived from Sup35 protein
QU Protein and Peptide Letters 2004 Feb; 11(1): 23-8
PT journal article
AB 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.
MH Amides/chemistry; Magnetic Resonance Spectroscopy; Peptide Fragments/*chemistry; Prions/*chemistry; Protons; Saccharomyces cerevisiae Proteins/*chemistry; Support, Non-U.S. Gov't; Support, U.S. Gov't, Non-P.H.S.; Support, U.S. Gov't, P.H.S.; Temperature
AD Department of Applied Chemistry and Recombinant Protein Expression Center, Sejong University, 98 Gunja-Dong, Gwangjin-Gu, Seoul, Korea, 143-747.
SP englisch
PO Niederlande