Backbone 1H and 13C Chemical Shift Assignments of murine prion protein (residues 121-232) in its reduced state

(2R)-2-amino-3-methylsulfanyl-propanoic acid

Chemical shift referencing was done using TSP as DSS caused aggregation of hPrP(121-230).

The unfolded state of the murine prion protein and properties of single-point mutants related to human prion diseases.

Thiol groups of C179 and C214 have been methylated.
Construct constitutes C-terminal domain (residues 121-232). First two residues are a remnant of the N-terminal (his)6 tag.

Schwalbe group, Goethe University Frankfurt