Identification and characterization of a gas-phase complex of methylenecyclopropane and chlorine monofluoride by rotational spectroscopy

1997 ◽  
Vol 93 (24) ◽  
pp. 4253-4258 ◽  
Author(s):  
Stephen A. Cooke ◽  
John H. Holloway ◽  
A. C. Legon
Keyword(s):  
Gas Phase ◽  
Rotational Spectroscopy ◽  
Phase Complex ◽  
Identification And Characterization

Accurate Characterization of the Peptide Linkage in the Gas Phase: A Joint Quantum-Chemical and Rotational Spectroscopy Study of the Glycine Dipeptide Analogue

2014 ◽  
Vol 5 (3) ◽  
pp. 534-540 ◽  
Author(s):  
Cristina Puzzarini ◽  
Malgorzata Biczysko ◽  
Vincenzo Barone ◽  
Laura Largo ◽  
Isabel Peña ◽  
...  
Keyword(s):  
Gas Phase ◽  
Quantum Chemical ◽  
Rotational Spectroscopy ◽  
Spectroscopy Study ◽  
Peptide Linkage

scholarly journals Deeper Protein Identification by Using FAIMS in Top-down Proteomics

2021 ◽  
Author(s):  
Robert Gerbasi ◽  
Rafael D. Melani ◽  
Susan E. Abbatiello ◽  
Michael W. Belford ◽  
Romain Huguet ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Molecular Weight ◽  
Gas Phase ◽  
Ion Mobility ◽  
Protein Identification ◽  
Signal To Noise ◽  
Top Down ◽  
Gas Phase Separation ◽  
Identification And Characterization

<div> <p>Field Asymmetric Ion Mobility Spectrometry (FAIMS), when used in proteomics studies, provides superior selectivity, and enables more proteins to be identified by providing additional gas phase separation. Here, we tested the performance of cylindrical FAIMS for the identification and characterization of proteoforms by top-down mass spectrometry of heterogeneous protein mixtures. Combining FAIMS with chromatographic separation resulted in a 62% increase in protein identifications and an 8% increase in proteoform identifications as compared to samples analyzed without FAIMS. This increase was attributable, in part, to improved signal-to-noise for proteoforms with similar retention times. Additionally, our results show that the optimal compensation voltage of any given proteoform was correlated with the molecular weight of the analyte. Collectively these results suggest that the addition of FAIMS can enhance top-down proteomics in both discovery and targeted applications. </p> </div>

scholarly journals Deeper Protein Identification by Using FAIMS in Top-down Proteomics

2021 ◽  
Author(s):  
Robert Gerbasi ◽  
Rafael D. Melani ◽  
Susan E. Abbatiello ◽  
Michael W. Belford ◽  
Romain Huguet ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Molecular Weight ◽  
Gas Phase ◽  
Ion Mobility ◽  
Protein Identification ◽  
Signal To Noise ◽  
Top Down ◽  
Gas Phase Separation ◽  
Identification And Characterization

<div> <p>Field Asymmetric Ion Mobility Spectrometry (FAIMS), when used in proteomics studies, provides superior selectivity, and enables more proteins to be identified by providing additional gas phase separation. Here, we tested the performance of cylindrical FAIMS for the identification and characterization of proteoforms by top-down mass spectrometry of heterogeneous protein mixtures. Combining FAIMS with chromatographic separation resulted in a 62% increase in protein identifications and an 8% increase in proteoform identifications as compared to samples analyzed without FAIMS. This increase was attributable, in part, to improved signal-to-noise for proteoforms with similar retention times. Additionally, our results show that the optimal compensation voltage of any given proteoform was correlated with the molecular weight of the analyte. Collectively these results suggest that the addition of FAIMS can enhance top-down proteomics in both discovery and targeted applications. </p> </div>

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