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Stepwise Evolution of Protein Native Structure with Electrospray into the Gas Phase, 10⁻¹² to 10² s
Kathrin Breuker and Fred W. McLafferty
Proceedings of the National Academy of Sciences of the United States of America
Vol. 105, No. 47 (Nov. 25, 2008), pp. 18145-18152
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/25465429
Page Count: 8
You can always find the topics here!Topics: Ions, Mass spectroscopy, Vapor phases, Cytochromes, Ubiquitins, Proteins, Biomolecules, Solvents, Electrostatics, Protein refolding
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Mass spectrometry (MS) has been revolutionized by electrospray ionization (ESI), which is sufficiently "gentle" to introduce nonvolatile biomolecules such as proteins and nucleic acids (RNA or DNA) into the gas phase without breaking covalent bonds. Although in some cases noncovalent bonding can be maintained sufficiently for ESI/MS characterization of the solution structure of large protein complexes and native enzyme/substrate binding, the new gaseous environment can ultimately cause dramatic structural alterations. The temporal (picoseconds to minutes) evolution of native protein structure during and after transfer into the gas phase, as proposed here based on a variety of studies, can involve side-chain collapse, unfolding, and refolding into new, non-native structures. Control of individual experimental factors allows optimization for specific research objectives.
Proceedings of the National Academy of Sciences of the United States of America © 2008 National Academy of Sciences