Kinetic intermediates in amyloid assemblyJournal of the American Chemical Society
AbstractIn contrast to an expected Ostwald-like ripening of amyloid assemblies, the nucleating core of the Dutch mutant of the Aβ peptide of Alzheimer’s disease assembles through a series of conformational transitions. Structural characterization of the intermediate assemblies by isotope-edited IR and solid-state NMR reveals unexpected strand orientation intermediates and suggests new nucleation mechanisms in a progressive assembly pathway.
Published CitationLiang, C. ‡, Ni, R. ‡, Smith, J. E. ‡, Childers, W. S., Mehta, A. K., Lynn, D. G. Kinetic intermediates in amyloid assembly. Journal of the American Chemical Society 136, no. 43 (October 2014): 15146-15149. 10.1021/ja508621b
Citation InformationChen Liang, Rong Ni, Jillian E. Smith-Carpenter, W. Seth Childers, et al.. "Kinetic intermediates in amyloid assembly" Journal of the American Chemical Society Vol. 136 Iss. 43 (2014)
Available at: http://works.bepress.com/jillian-smith-carpenter/1/