Expression yielded large amounts of soluble protein in the periplasmic fraction. For efficient cleavage of the OmpA signal sequence by leader peptidase, a serine residue was inserted at the aminoterminus of the recombinant PrP fragments. This suggested that the segment 121-231, which is resistant to degradation in the periplasm of E. coli, represents an intrinsically stable domain and that residues 108 to 120 are not part of this domain. A protein-folding reaction under kinetic control. Mice devoid of PrP are resistant to scrapie.
Prion protein is necessary for normal synaptic function.
Conformational polymorphism of the amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein. Conformational pathway of the polypeptide chain of chymotrypsin inhibitor-2 growing from its N terminus in vitro. Parallels with the protein folding pathway. Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding.