NR AEQD
AU Glover,K.J.; Whiles,J.A.; Wood,M.J.; Melacini,G.; Komives,E.A.; Vold,R.R.
TI Conformational dimorphism and transmembrane orientation of prion protein residues 110-136 in bicelles
QU Biochemistry 2001 Nov 6; 40(44): 13137-42
PT journal article
AB 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. Amide-lipid NOEs and amide-water chemical exchange measurements revealed that the helical conformation of prion(110-136) spanned the bilayer, and were corroborated by solid-state deuterium NMR experiments indicating that the helical axis rested at a 16 degrees angle with respect to the bilayer normal.
MH Animal; Cell Membrane/chemistry; Circular Dichroism; Lipid Bilayers; Magnetic Resonance Spectroscopy; Peptide Fragments/chemical synthesis/*chemistry/isolation & purification; Phosphatidylcholines/chemistry; Prions/*chemistry; Protein Conformation; Spectrometry, Fluorescence; Support, U.S. Gov't, Non-P.H.S.; Support, U.S. Gov't, P.H.S.
AD Department of Chemistry and Biochemistry, 0359, University of California at San Diego, 9500 Gilman Drive, La Jolla, California 92093-0359, USA
SP englisch
PO USA