NR AJZU
AU Riek,R.; Hornemann,S.; Wider,G.; Glockshuber,R.; Wüthrich,K.
TI NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231)
QU FEBS Letters 1997 Aug 18; 413(2): 282-8
PT journal article
AB The recombinant murine prion protein, mPrP(23-231), was expressed in E. coli with uniform 15N-labeling. NMR experiments showed that the previously determined globular three-dimensional structure of the C-terminal domain mPrP(121-231) is preserved in the intact protein, and that the N-terminal polypeptide segment 23-120 is flexibly disordered. This structural information is based on nearly complete sequence-specific assignments for the backbone amide nitrogens, amide protons and alpha-protols of the polypeptide segment of residues 121-231 in mPrP(23-231). Coincidence of corresponding sequential and medium-range nuclear Overhauser effects (NOE) showed that the helical secondary structures previously identified in mPrP(121-231) are also present in mPrP(23-231), and near-identity of corresponding amide nitrogen and amide proton chemical shifts indicates that the three-dimensional fold of mPrP(121-231) is also preserved in the intact protein. The linewidths in heteronuclear 1H-15N correlation spectra and 15N[1H]-NOEs showed that the well structured residues 126-230 have correlation times of several nanoseconds, as is typical for small globular proteins, whereas correlation times shorter than 1 nanosecond were observed for all residues of mPrP(23-231) outside of this domain.
MH Amino Acid Sequence; Animal; Magnetic Resonance Spectroscopy/*methods; Mice; Models, Molecular; Molecular Sequence Data; PrPc Proteins/*chemistry; Protein Conformation; *Protein Structure, Secondary; Recombinant Fusion Proteins/chemistry; Support, Non-U.S. Gov't
AD Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule-Honggerberg, Zürich, Switzerland.
SP englisch
PO Niederlande