Journal article
Conformational Dimorphism and Transmembrane Orientation of Prion Protein Residues 110−136 in Bicelles †
Abstract
A fragment corresponding to the putative membrane-associating domain of the prion protein (residues 110-136) was analyzed in phospholipid bicelles. Prion(110-136) associated with bicelles and exhibited a lipid- and pH-dependent conformational dimorphism between unstructured (pH 4.5) and alpha-helical (pH 7.5). Mutational analysis indicated that the charge state of a single histidine residue was largely responsible for the dimorphism. …
Authors
Glover KJ; Whiles JA; Wood MJ; Melacini G; Komives EA; Vold RR
Journal
Biochemistry, Vol. 40, No. 44, pp. 13137–13142
Publisher
American Chemical Society (ACS)
Publication Date
November 1, 2001
DOI
10.1021/bi011485m
ISSN
0006-2960