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.
Dates
Type | When |
---|---|
Created | 19 years, 2 months ago (May 31, 2006, 9:29 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 2:07 p.m.) |
Indexed | 1 month, 2 weeks ago (July 2, 2025, 1:52 p.m.) |
Issued | 30 years, 4 months ago (March 28, 1995) |
Published | 30 years, 4 months ago (March 28, 1995) |
Published Online | 30 years, 4 months ago (March 28, 1995) |
Published Print | 30 years, 4 months ago (March 28, 1995) |
@article{Wood_1995, title={Gas-phase folding and unfolding of cytochrome c cations.}, volume={92}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.92.7.2451}, DOI={10.1073/pnas.92.7.2451}, number={7}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Wood, T D and Chorush, R A and Wampler, F M and Little, D P and O’Connor, P B and McLafferty, F W}, year={1995}, month=mar, pages={2451–2454} }