Conformational stability of Syrian hamster prion protein PrP(90-231).
Many transmissible spongiform encephalopathies (TSEs) are believed to be caused by a misfolded form of the normal cellular prion protein (PrP(C)) known as PrP(Sc). While PrP(Sc) is known to be exceptionally stable and resistant to protease degradation, PrP(C) has not shown these same unusual characteristics. However, using ion mobility spectrometry mass spectrometry (IMS-MS), we found evidence for at least one very stable conformation of a truncated form of recombinant PrP(C) consisting of residues 90-231, which resists unfolding in the absence of solvent at high injection energies and at temperatures in excess of 600 K. We also report the first absolute collision cross sections measured for recombinant Syrian hamster prion protein PrP(90-231).
Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106, USA.
Megan
M
Grabenauer
Thomas
T
Wyttenbach
Narinder
N
Sanghera
Susan E
SE
Slade
Teresa J T
TJ
Pinheiro
James H
JH
Scrivens
Michael T
MT
Bowers
D000818:Animals; D006224:Cricetinae; D006863:Hydrogen-Ion Concentration; D013058:Mass Spectrometry; D008647:Mesocricetus; D010446:Peptide Fragments / Q000737:chemistry*; D011328:Prions / Q000737:chemistry*; D055550:Protein Stability; D017433:Protein Structure, Secondary; D013696:Temperature
D010446:Peptide Fragments; D011328:Prions; C507417:prion protein (90-231)