NR ARMJ
AU Krebs,M.R.H.; Morozova-Roche,L.A.; Daniel,K.; Robinson,C.V.; Dobson,C.M.
TI Observation of sequence specificity in the seeding of protein amyloid fibrils
QU Protein Science 2004 Jul; 13(7): 1933-8
IA http://www.proteinscience.org/cgi/content/full/13/7/1933
PT journal article
AB It is well established that the rate of formation of fibrils by amyloidogenic proteins is enhanced by the addition of preformed fibrils, a phenomenon known as seeding. We show that the efficiency of seeding fibril formation from solutions of hen lysozyme by a series of other proteins depends strongly on the similarity of their sequences. This observation is consistent with the importance of long-range interactions in stabilizing the core structure of amyloid fibrils and may be associated with the existence of a species barrier observed in the transmissible spongiform encephalopathies. In addition, it is consistent with the observation of a single dominant type of protein in the deposits associated with each form of amyloid disease.
MH Animals; Chickens; Multiprotein Complexes/*chemistry/metabolism/ultrastructure; Muramidase/*chemistry/metabolism; Prion Diseases/metabolism; Protein Folding; Research Support, Non-U.S. Gov't; Species Specificity; Spectrum Analysis
AD Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
SP englisch
PO USA