Unfolding of proteins monitored by electrospray ionization mass spectrometry: a comparison of positive and negative ion modes
- 1 December 1998
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Society for Mass Spectrometry
- Vol. 9 (12) , 1248-1254
- https://doi.org/10.1016/s1044-0305(98)00103-2
Abstract
No abstract availableKeywords
This publication has 52 references indexed in Scilit:
- Acid-Induced Denaturation of Myoglobin Studied by Time-Resolved Electrospray Ionization Mass SpectrometryBiochemistry, 1997
- Do proteins denature during droplet evolution in electrospray ionization?International Journal of Mass Spectrometry and Ion Processes, 1997
- Changes in bulk solution pH caused by the inherent controlled-current electrolytic process of an electrospray ion sourceInternational Journal of Mass Spectrometry and Ion Processes, 1997
- Dissecting the Structure of a Partially Folded Protein: Circular Dichroism and Nuclear Magnetic Resonance Studies of Peptides from UbiquitinJournal of Molecular Biology, 1993
- Hydrogen/deuterium exchange electrospray ionization mass spectrometry: a method for probing protein conformational changes in solutionJournal of the American Chemical Society, 1993
- Electrospray mass spectrometry of some proteins and the aqueous solution acid/base equilibrium model in the negative ion detection modeInternational Journal of Mass Spectrometry and Ion Processes, 1993
- Heat-induced conformational changes in proteins studied by electrospray ionization mass spectrometryAnalytical Chemistry, 1993
- Characterization of a partially denatured state of a protein by two-dimensional NMR: reduction of the hydrophobic interactions in ubiquitinBiochemistry, 1991
- Structure of ubiquitin refined at 1.8 Å resolutionJournal of Molecular Biology, 1987
- Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroismJournal of Molecular Biology, 1980