Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 55, Issue 45, Pages 14173-14176Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201606029
Keywords
gas-phase reactions; IR spectroscopy; mass spectrometry; protein folding; protein structures
Categories
Funding
- National Science Foundation (USA) [CHE-1301032]
- Alexander von Humboldt foundation
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1301032] Funding Source: National Science Foundation
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Can the structures of small to medium-sized proteins be conserved after transfer from the solution phase to the gas phase? A large number of studies have been devoted to this topic, however the answer has not been unambiguously determined to date. A clarification of this problem is important since it would allow very sensitive native mass spectrometry techniques to be used to address problems relevant to structural biology. A combination of ion-mobility mass spectrometry with infrared spectroscopy was used to investigate the secondary and tertiary structure of proteins carefully transferred from solution to the gas phase. The two proteins investigated are myoglobin and -lactoglobulin, which are prototypical examples of helical and -sheet proteins, respectively. The results show that for low charge states under gentle conditions, aspects of the native secondary and tertiary structure can be conserved.
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