Journal
CHEMBIOCHEM
Volume 9, Issue 15, Pages 2417-2423Publisher
WILEY-BLACKWELL
DOI: 10.1002/cbic.200800167
Keywords
desolvation; electrospray ionization; molecular dynamics; native electron capture dissociation; protein structures
Funding
- Austrian FWF [V59-N11, Y372-N17]
- NIH [GM59796, GM16609]
- Austrian Science Fund (FWF) [Y 372] Funding Source: researchfish
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Electrospray ionization transfers thermally labile biomolecules, such as proteins, from solution into the gas phase, where they can be studied by mass spectrometry. Covalent bonds are generally preserved during and after the phase transition, but it is less clear to what extent noncovalent interactions are affected by the new gaseous environment. Here, we present atomic-level computational data on the structural rearrangement of native cytochrome c immediately after solvent removal. The first structural changes after desolvation occur surprisingly early, on a timescale of picoseconds. For the time segment of up to 4.2 ns investigated here, we observed no significant breaking of native noncovalent bonds instead, we found formation of new noncovalent bonds. This generally involves charged residues on the protein surface, resulting in transiently stabilized intermediate structures with a global fold that is essentially the same as that in solution. Comparison with data from native electron capture dissociation experiments corroborates both its mechanistic postulations and our computational predictions, and suggests that global structural changes take place on a millisecond timescale not covered by our simulations.
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