Gas-phase folding and unfolding of cytochrome c cations.
- 28 March 1995
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 92 (7) , 2451-2454
- https://doi.org/10.1073/pnas.92.7.2451
Abstract
Water is thought to play a dominant role in protein folding, yet gaseous multiply protonated proteins from which the water has been completely removed show hydrogen/deuterium (H/D) exchange behavior similar to that used to identify conformations in solution. Indicative of the gas-phase accessibility to D2O, multiply-charged (6+ to 17+) cytochrome c cations exchange at six (or more) distinct levels of 64 to 173 out of 198 exchangeable H atoms, with the 132 H level found at charge values 8+ to 17+. Infrared laser heating and fast collisions can apparently induce ions to unfold to exchange at a higher distinct level, while charge-stripping ions to lower charge values yields apparent folding as well as unfolding.Keywords
This publication has 17 references indexed in Scilit:
- Infrared Multiphoton Dissociation of Large Multiply Charged Ions for Biomolecule SequencingAnalytical Chemistry, 1994
- Does folding determine protein configuration?Nature, 1994
- Conformation of Cytochrome c Studied by Deuterium Exchange-Electrospray Ionization Mass SpectrometryAnalytical Chemistry, 1994
- Detection of Transient Protein Folding Populations by Mass SpectrometryScience, 1993
- In Pursuit of Protein FoldingScience, 1993
- Two-dimensional proton NMR studies of cytochrome c: hydrogen exchange in the N-terminal helixBiochemistry, 1986
- Energetics of protein structure and foldingBiopolymers, 1985
- Exchange of individual hydrogens for a protein in a crystal and in solutionJournal of Molecular Biology, 1983
- Detection of three kinetic phases in the thermal unfolding of ferricytochrome cBiochemistry, 1973
- Hydrogen Exchange in ProteinsAdvances in Protein Chemistry, 1966