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
2005 ◽  
Vol 83 (11) ◽  
pp. 1961-1968 ◽  
Author(s):  
Randy W Purves ◽  
Barbara Ells ◽  
David A Barnett ◽  
Roger Guevremont

Conformers of equine cytochrome c were investigated in the gas phase using a combination of high-field asymmetric waveform ion mobility spectrometry (FAIMS) and hydrogen–deuterium (H–D) exchange. Electrospray generated ions of equine cytochrome c were exposed to a low concentration of D2O vapour while being transported by a flow of nitrogen through a FAIMS device. During this transport period of about 250 ms in the FAIMS analyzer, the various conformers of multiply charged ions of cytochrome c were simultaneously undergoing H–D exchange and being separated from each other. The extent of H–D exchange was calculated from the observed m/z of conformers after exposure to D2O vapour in FAIMS. The complementary nature of these two methods resulted in observations supporting a greater number of conformers (e.g., at least 11 conformers were identified for the +16 charge state) than would be expected by analyzing the FAIMS data and the H–D exchange data independently.Key words: FAIMS, H–D exchange, mass spectrometry, protein conformations, electrospray ionization.


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

2013 ◽  
Vol 135 (16) ◽  
pp. 6078-6083 ◽  
Author(s):  
Antoni J. Borysik ◽  
Dominic J. Hewitt ◽  
Carol V. Robinson

2018 ◽  
Author(s):  
Charles Eldrid ◽  
Jakub Ujma ◽  
Symeon Kalfas ◽  
nick tomczyk ◽  
Kevin Giles ◽  
...  

<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>


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):  

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