Gas-phase folding and unfolding of cytochrome c cations

Troy D. Wood; Russell A. Chorush; Francis M. Wampler; Daniel P. Little; Peter B. O'Connor; Fred W. McLafferty

doi:10.1073/pnas.92.7.2451

Gas-phase folding and unfolding of cytochrome c cations

Troy D. Wood
, Russell A. Chorush
, Francis M. Wampler
, Daniel P. Little
, Peter B. O'Connor
, Fred W. McLafferty

Chemistry

Cornell University

Research output: Contribution to journal › Article › peer-review

269 Scopus citations

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.

Original language	English
Pages (from-to)	2451-2454
Number of pages	4
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	92
Issue number	7
DOIs	https://doi.org/10.1073/pnas.92.7.2451
State	Published - Mar 28 1995

Keywords

deuterium exchange
electrospray ionization
Fourier-transform mass spectrometry
hydrogen
protein conformation

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10.1073/pnas.92.7.2451

Cite this

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title = "Gas-phase folding and unfolding of cytochrome c cations",

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.",

keywords = "deuterium exchange, electrospray ionization, Fourier-transform mass spectrometry, hydrogen, protein conformation",

author = "Wood, \{Troy D.\} and Chorush, \{Russell A.\} and Wampler, \{Francis M.\} and Little, \{Daniel P.\} and O'Connor, \{Peter B.\} and McLafferty, \{Fred W.\}",

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doi = "10.1073/pnas.92.7.2451",

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T1 - Gas-phase folding and unfolding of cytochrome c cations

AU - Wood, Troy D.

AU - Chorush, Russell A.

AU - Wampler, Francis M.

AU - Little, Daniel P.

AU - O'Connor, Peter B.

AU - McLafferty, Fred W.

PY - 1995/3/28

Y1 - 1995/3/28

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AB - 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.

KW - deuterium exchange

KW - electrospray ionization

KW - Fourier-transform mass spectrometry

KW - hydrogen

KW - protein conformation

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JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

IS - 7

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Gas-phase folding and unfolding of cytochrome c cations

Abstract

Keywords

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