Gerhard Wider

TL;DR: The TROSY principle should benefit a variety of multidimensional solution NMR experiments, especially with future use of yet somewhat higher polarizing magnetic fields than are presently available, and thus largely eliminate one of the key factors that limit work with larger molecules.

TL;DR: The nuclear magnetic resonance (NMR) structure of the autonomously folding PrP domain contains most of the point-mutation sites that have been linked, in human PrP, to the occurrence of familial prion diseases, and shows that these mutations occur within, or directly adjacent to, regular secondary structures.

TL;DR: The NMR structures of the recombinant human prion protein hPrP(23-230) include a globular domain extending from residues 125-228, for which a detailed structure was obtained, and an N-terminal flexibly disordered "tail," which influences the local conformational state of the polypeptide segments.

TL;DR: In this article, the identification of two ubiquitin (Ub)-binding domains (UBM and UBZ), which are evolutionarily conserved in all Y-family TLS polymerases (pols), is described.

TL;DR: The recombinant murine prion protein, mPrP(23-231), was expressed in E. coli with uniform 15N-labeling and 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 Nterminal polypeptide segment 23-120 is flexibly disordered as mentioned in this paper, based on nearly complete sequence-specific assignments for the backbone amide nitrogens, amide protons and alpha-protols of