Free energy for blue copper protein unfolding determined by electrospray ionisation mass spectrometry
- 5 September 2001
- journal article
- Published by Wiley in Rapid Communications in Mass Spectrometry
- Vol. 15 (19) , 1817-1825
- https://doi.org/10.1002/rcm.439
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- Probing the Non-covalent Structure of Proteins by Amide Hydrogen Exchange and Mass SpectrometryJournal of Mass Spectrometry, 1997
- Mass Spectrometric Determination of Isotopic Exchange Rates of Amide Hydrogens Located on the Surfaces of ProteinsAnalytical Chemistry, 1996
- Conformational Heterogeneity and Stability of Apomyoglobin Studied by Hydrogen/Deuterium Exchange and Electrospray Ionization Mass SpectrometryBiochemistry, 1996
- Kinetic Consequences of the Removal of a Disulfide Bridge on the Folding of Hen LysozymeBiochemistry, 1994
- Solution Structure of the Type 1 Blue Copper Protein Amicyanin from Thiobacillus versutusJournal of Molecular Biology, 1994
- Crystal structure analysis and refinement at 2·15Å resolution of amicyanin, a type I blue copper protein, from Thiobacillus versutusJournal of Molecular Biology, 1994
- Detection of Transient Protein Folding Populations by Mass SpectrometryScience, 1993
- Hydrogen/deuterium exchange electrospray ionization mass spectrometry: a method for probing protein conformational changes in solutionJournal of the American Chemical Society, 1993
- Heat-induced conformational changes in proteins studied by electrospray ionization mass spectrometryAnalytical Chemistry, 1993
- Detection of noncovalent receptor-ligand complexes by mass spectrometryJournal of the American Chemical Society, 1991