Mouse prion protein fragment 121-231 AT 37 C
Cellular prion protein conformation and function.
GSVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENF TETDVKMMERVVEQMCVTQYQKESQAYYDGRRSS
Additional HN/N signals from the beta 2-alpha 2 loop of the mouse prion protein fragment 121-231 are visible at 37C allowing the identification of additional NOE constraints which lead to a defined conformation for the loop.
MOUSE PRION PROTEIN FRAGMENT 121-231 AT 20 C
MOUSE PRION PROTEIN (121-231) CONTAINING THE SUBSTITUTION Y169G
MOUSE PRION PROTEIN (121-231) CONTAINING THE SUBSTITUTION F175A
MOUSE PRION PROTEIN (121-231) CONTAINING THE SUBSTITUTIONS Y169A, Y225A, AND Y226A
RESIDUES GLY A 119 AND SER A 120 ARE LEFT OVER FROM THE THROMBIN CLEAVAGE OF THE HIS TAG
Two 13C-resolved [1H,1H]-NOESY spectra were obtained with the 13C carrier and spectral width optimized for aliphatic and aromatic 13C resonances respectively.
Luginbuhl, Guntert, Billeter and Wuthrich
prion, conformational exchange, MEMBRANE PROTEIN
VVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTE TDVKMMERVVEQMCVTQYQKESQAYYDGRRSS