Measurement of Very Fast Exchange Rates of Individual Amide Protons in Proteins by NMR Spectroscopy
Author:
Affiliation:
1. Department of Chemistry, and Interdisciplinary Nanoscience Center (iNANO); Aarhus University; 8000 Aarhus Denmark
2. Department of Chemistry; University of Florence; 50019 Sesto Fiorentino, (FI) Italy
Funder
Danish Center for Ultra-High Field NMR Spectroscopy
Publisher
Wiley
Subject
Physical and Theoretical Chemistry,Atomic and Molecular Physics, and Optics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/cphc.201801044/fullpdf
Reference43 articles.
1. Protein structure change studied by hydrogen-deuterium exchange, functional labeling, and mass spectrometry
2. Protein stability parameters measured by hydrogen exchange
3. Identifying protein folding cores from the evolution of flexible regions during unfolding
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