Recently, a general picture has been proposed of how long, and to what extent, native protein structure can be retained in the gas phase.1a In particular, molecular dynamics simulations suggest that salt bridges and ionic hydrogen bonds on the protein surface can transiently stabilize the global fold shortly after desolvation.1b However, the use of native mass spectrometry2 for studying protein solution structure is still controversial, mostly because site-specific experimental gas-phase data3 is scarce. Here we report electron capture dissociation (ECD)4 data on the gas-phase structures of the three-helix bundle protein KIX5 (Figure 1) that indicate substantial preservation of the native solution structure on a timescale of at least 4 s. We demonstrate that in the gas phase, the most stable regions are those stabilized by salt bridges and ionic hydrogen bonds.
Electrostatic Stabilization of a Native Protein Structure in the Gas Phase**
K. Breuker,Sven Brüschweiler,M. Tollinger
Published 2010 in Angewandte Chemie
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- Publication year
2010
- Venue
Angewandte Chemie
- Publication date
2010-11-09
- Fields of study
Medicine, Chemistry
- Identifiers
- External record
- Source metadata
Semantic Scholar, PubMed
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