Paper Citing NAMD - Abstract
Lam, A. R.; Jiang, J.; Mukamel, S.
Distinguishing Amyloid Fibril Structures in Alzheimer's Disease (AD) by Two-Dimensional Ultraviolet (2DUV) Spectroscopy
BIOCHEMISTRY, 50:9809-9816, NOV 15 2011
Understanding the aggregation mechanism of amyloid fibrils and characterizing their structures are important steps in the investigation of several neurodegenerative disorders associated with the misfolding of proteins. We report a simulation study of coherent two-dimensional chiral signals of three NMR structures of A beta protein fibrils associated with Alzheimer's Disease, two models for A beta(8-40) peptide wild-type (WT) and one for the Iowa (D23N) A beta(15-40) mutant. Both far-ultraviolet (FUV) signals (lambda = 190-250 nm), which originate from the backbone n pi* and pi pi* transitions, and near-ultraviolet (NUV) signals (lambda >= 250 nm) associated with aromatic side chains (Phe and Tyr) show distinct cross-peak patterns that can serve as novel signatures for the secondary structure.
