GYVLGS segment 127-132 from human prion with V129
Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease.
0.1M Sodium Acetate pH 5.5, PEG 10,000, vapor diffusion, hanging drop, temperature 298K
GYVLGS (residues 127-132 with V129) from human prion protein, synthesized
HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
amyloid-like protofibril, PROTEIN FIBRIL