Conformational properties of Rhodobacter capsulatus cytochrome c2 wild‐type and site‐directed mutants using hydrogen/deuterium exchange monitored by electrospray ionization mass spectrometry
- 1 January 1995
- journal article
- research article
- Published by Wiley in Rapid Communications in Mass Spectrometry
- Vol. 9 (12) , 1135-1140
- https://doi.org/10.1002/rcm.1290091211
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Hydrogen exchange rates and protein foldingCurrent Opinion in Structural Biology, 1994
- Site-specific mutagenesis studies of cytochromes cBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1994
- Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidationProtein Science, 1993
- Heat-induced conformational changes in proteins studied by electrospray ionization mass spectrometryAnalytical Chemistry, 1993
- Determination of amide hydrogen exchange rates in peptides by mass spectrometryAnalytical Chemistry, 1992
- Protein structural effects in gas phase ion/molecule reactions with diethylamineRapid Communications in Mass Spectrometry, 1992
- Molecular structure of cytochrome c2 isolated from Rhodobacter capsulatus determined at 2·5 Å resolutionJournal of Molecular Biology, 1991
- Comparison of amide proton exchange in reduced and oxidizedRhodobacter capsulatus cytochrome c2: A1H−15N NMR studyJournal of Biomolecular NMR, 1991
- A spectroscopic analysis of the Pro35 → Ala mutant of Rhodobacter capsulatus cytochrome c2European Journal of Biochemistry, 1991
- Solvent‐induced conformational changes of polypeptides probed by electrospray‐ionization mass spectrometryRapid Communications in Mass Spectrometry, 1991