scholarly journals Separation of biologically relevant isomers on an Orbitrap mass spectrometer using high‐resolution drift tube ion mobility and varied drift gas mixtures

2019 ◽  
Vol 33 (S2) ◽  
pp. 3-10 ◽  
Author(s):  
Julia L. Kaszycki ◽  
Aurelio La Rotta ◽  
Benoit Colsch ◽  
François Fenaille ◽  
Claire Dauly ◽  
...  
2014 ◽  
Vol 86 (4) ◽  
pp. 2107-2116 ◽  
Author(s):  
Jody C. May ◽  
Cody R. Goodwin ◽  
Nichole M. Lareau ◽  
Katrina L. Leaptrot ◽  
Caleb B. Morris ◽  
...  

The Analyst ◽  
2015 ◽  
Vol 140 (20) ◽  
pp. 6904-6911 ◽  
Author(s):  
M. Groessl ◽  
S. Graf ◽  
R. Knochenmuss

Separation and identification of isomeric species is a major challenge in lipidomics. Herein, we demonstrate that lipid isomers that differ only in position of the acyl chain, position of the double bond or double bond geometry can be distinguished using drift-tube ion mobility-mass spectrometry, even in complex biological samples.


2009 ◽  
Vol 23 (10) ◽  
pp. 1411-1418 ◽  
Author(s):  
Albert Koulman ◽  
Gary Woffendin ◽  
Vinod K. Narayana ◽  
Helen Welchman ◽  
Catharina Crone ◽  
...  

2019 ◽  
Author(s):  
Dorte B. Bekker-Jensen ◽  
Ana Martínez del Val ◽  
Sophia Steigerwald ◽  
Patrick Rüther ◽  
Kyle Fort ◽  
...  

ABSTRACTState-of-the-art proteomics-grade mass spectrometers can measure peptide precursors and their fragments with ppm mass accuracy at sequencing speeds of tens of peptides per second with attomolar sensitivity. Here we describe a compact and robust quadrupole-orbitrap mass spectrometer equipped with a front-end High Field Asymmetric Waveform Ion Mobility Spectrometry (FAIMS) Interface. The performance of the Orbitrap Exploris 480 mass spectrometer is evaluated in data-dependent acquisition (DDA) and data-independent acquisition (DIA) modes in combination with FAIMS. We demonstrate that different compensation voltages (CVs) for FAIMS are optimal for DDA and DIA, respectively. Combining DIA with FAIMS using single CVs, the instrument surpasses 2500 unique peptides identified per minute. This enables quantification of >5000 proteins with short online LC gradients delivered by the Evosep One LC system allowing acquisition of 60 samples per day. The raw sensitivity of the instrument is evaluated by analyzing 5 ng of a HeLa digest from which >1000 proteins were reproducibly identified with 5 minute LC gradients using DIA-FAIMS. To demonstrate the versatility of the instrument we recorded an organ-wide map of proteome expression across 12 rat tissues quantified by tandem mass tags and label-free quantification using DIA with FAIMS to a depth of >10,000 proteins.


Xenobiotica ◽  
2020 ◽  
Vol 50 (12) ◽  
pp. 1423-1433
Author(s):  
Su Min Choi ◽  
Younah Kim ◽  
Jaeick Lee ◽  
Ju-Hyun Kim ◽  
Taeho Lee ◽  
...  

2015 ◽  
Vol 72 ◽  
pp. 278-282 ◽  
Author(s):  
D.M. Chernyshev ◽  
S.S. Poteshin ◽  
A.V. Karpov ◽  
Alexey A. Sysoev ◽  
Alexander A. Sysoev

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