Toward a proper interpretation of hydrogen exchange data in disordered proteins
Author:
Funder
Saint Petersburg State University
Publisher
Elsevier BV
Subject
Biophysics
Reference11 articles.
1. Hydrogen exchange identifies native-state motional domains important in protein folding;Kim;Biochemistry,1993
2. Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH;Chamberlain;Nat. Struct. Biol,1996
3. Measuring hydrogen exchange rates in invisible protein excited states;Long;Proc. Natl. Acad. Sci. USA,2014
4. Structural differences in Aβ amyloid protofibrils and fibrils mapped by hydrogen exchange – mass spectrometry with on-line proteolytic fragmentation;Kheterpal;J. Mol. Biol,2006
5. Distinct aggregation mechanisms of monoclonal antibody under thermal and freeze-thaw stresses revealed by hydrogen exchange;Zhang;Pharm. Res,2012
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