Insights into the role of the beta-2 microglobulin D-strand in amyloid propensity revealed by mass spectrometry
Author:
Affiliation:
1. Astbury Centre for Structural Molecular Biology and School of Molecular and Cellular Biology
2. Faculty of Biological Sciences
3. University of Leeds
4. Leeds, UK
Abstract
Characterising the differences between oligomers formed from the amyloidogenic protein β2-microglobulin and its mutant H51A using ESI-IMS-MS.
Publisher
Royal Society of Chemistry (RSC)
Subject
Molecular Biology,Biotechnology
Link
http://pubs.rsc.org/en/content/articlepdf/2014/MB/C3MB70420C
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4. F. Chiti and C. M.Dobson , Protein misfolding, functional amyloid, and human disease , Annual Review of Biochemistry , Annual Reviews , Palo Alto , 2006 , pp. 333–366
5. A new form of amyloid protein associated with chronic hemodialysis was identified as β2-microglobulin
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