Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 132, Issue 18, Pages 6324-6328Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja909074j
Keywords
-
Categories
Funding
- National Science Foundation [CHE-0809525]
Ask authors/readers for more resources
Understanding fibrillogenesis at a molecular level requires detailed structural characterization of amyloid fibrils. The combination of deep UV resonance Raman (DUVRR) spectroscopy and post mortem hydrogen-deuterium exchange (HX) was utilized for probing parallel vs antiparallel beta-sheets in fibrils prepared from full-length A beta(1-40) and A beta(34-42) peptides, respectively. Using previously published structural data based on solid-state NMR analysis, we verified the applicability of Asher's approach for the quantitative characterization of peptide conformation in the A beta(1-40) fibril core. We found that the conformation of the parallel beta-sheet in the A beta(1-40) fibril core is atypical for globular proteins, while in contrast, the antiparallel beta-sheet in A beta(32-42) fibrils is a common structure in globular proteins. In contrast to the case for globular proteins, the conformations of parallel and antiparallel beta-sheets in A beta fibril cores are substantially different, and their differences can be distinguished by DUVRR spectroscopy.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available