Soret Band of the Gas-Phase Ferri-Cytochrome c

2012 ◽  
Vol 3 (6) ◽  
pp. 698-702 ◽  
Author(s):  
Claire Brunet ◽  
Rodolphe Antoine ◽  
Jérôme Lemoine ◽  
Philippe Dugourd
Keyword(s):  
Cytochrome C ◽  
Gas Phase ◽  
Soret Band

scholarly journals Evidence for unfolding and refolding of gas-phase cytochrome c ions in a Paul trap

2005 ◽  
Vol 16 (9) ◽  
pp. 1493-1497 ◽  
Author(s):  
Ethan R. Badman ◽  
Sunnie Myung ◽  
David E. Clemmer
Keyword(s):  
Cytochrome C ◽  
Gas Phase ◽  
Paul Trap

scholarly journals Gas Phase Stability of Protein Ions in a Cyclic Ion Mobility Spectrometry Travelling Wave Device

2018 ◽  
Author(s):  
Charles Eldrid ◽  
Jakub Ujma ◽  
Symeon Kalfas ◽  
nick tomczyk ◽  
Kevin Giles ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Gas Phase ◽  
Ion Mobility ◽  
Structural Changes ◽  
Structural Information ◽  
Travelling Wave ◽  
Resolving Power ◽  
Small Proteins ◽  
Multimeric Complex ◽  
Protein Ions

<div>Ion mobility mass spectrometry (IM-MS) allows separation of native protein ions into “conformational families”. Increasing the IM resolving power should allow finer structural information to be obtained, and can be achieved by increasing the length of the IM separator. This, however, increases the time that protein ions spend in the gas phase and previous experiments have shown that the initial conformations of small proteins can be lost within tens of milliseconds. Here, we report on investigations of protein ion stability using a multi-pass travelling wave (TW) cyclic IM (cIM) device. Using this device, minimal structural changes were observed for Cytochrome C after hundreds of milliseconds, while no changes were observed for a larger multimeric complex (Concanavalin A). The geometry of the instrument (Q-cIM-ToF) also enables complex tandem IM experiments to be performed which were used to obtain more detailed collision induced unfolding pathways for Cytochrome C. The novel instrument geometry provide unique capabilities with the potential to expand the field of protein analysis via IM-MS.</div>

A Polar Liquid Zwitterion Does Not Critically Destroy Cytochrome c at High Concentration: An Initial Comparative Study with a Polar Ionic Liquid

2019 ◽  
Vol 72 (2) ◽  
pp. 139 ◽  
Author(s):  
Kosuke Kuroda ◽  
Chiaki Kodo ◽  
Kazuaki Ninomiya ◽  
Kenji Takahashi
Keyword(s):  
Ionic Liquid ◽  
Cytochrome C ◽  
Soret Band ◽  
Liquid Solution ◽  
Acetate Solution ◽  
High Concentration ◽  
Liquid Solutions ◽  
High Concentration Range ◽  
Ionic Liquid Solution ◽  
Better Than

A polar carboxylate-type zwitterion with a small volume of water can dissolve cytochrome c without significant disruption, compared with the case of a popular polar carboxylate-type ionic liquid, 1-ethyl-3-methylimidazolium acetate. A change in the Soret, Q, and 615nm bands was not observed in the 80 wt-% polar zwitterion solution, whereas a shift in the Soret band, diminishing Q band, and appearance of the 615nm band was found in the 80 wt-% polar ionic liquid solution. It suggests that concentrated polar ionic liquid solutions critically disrupt the structure of cytochrome c, and the polar zwitterion solution used in this study was better than a 1-ethyl-3-methylimidazolium acetate solution in a high concentration range.

scholarly journals Gas-phase folding and unfolding of cytochrome c cations.

1995 ◽  
Vol 92 (7) ◽  
pp. 2451-2454 ◽  
Author(s):  
T. D. Wood ◽  
R. A. Chorush ◽  
F. M. Wampler ◽  
D. P. Little ◽  
P. B. O'Connor ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Gas Phase

Naked Protein Conformations: Cytochrome c in the Gas Phase

1995 ◽  
Vol 117 (40) ◽  
pp. 10141-10142 ◽  
Author(s):  
David E. Clemmer ◽  
Robert R. Hudgins ◽  
Martin F. Jarrold
Keyword(s):  
Cytochrome C ◽  
Gas Phase ◽  
Protein Conformations
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