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Chapter 4. Liquid Chromatography-Mass Spectrometry of Intact Proteins
2011In this chapter we address the use of liquid chromatography-mass spectrometry in the analysis of intact proteins. We cover multiple approaches and applications including quantitation, identification and the derivation of structural information. Because of the difficulty of intact protein analysis and the variety of approaches necessary for proteins of ...
Nicolas L. Young, Benjamin A. Garcia
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Investigating Viral Proteins and Intact Viruses with Mass Spectrometry
2003Mass spectrometry has become a fundamental technology for virology and an important tool in probing the structure and function of viruses. It has been used to identify viral capsid proteins, detect viral mutants, characterize post-translational modifications, and measure intact viruses. Mass-based analysis techniques including time resolved proteolysis,
Sunia A. Trauger +2 more
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Analytical Chemistry, 2018
Recent advances in the analysis of proteins have increased the demand for more efficient techniques to separate intact proteins. Enhanced-fluidity liquid chromatography (EFLC) involves the addition of liquefied CO2 to conventional liquid mobile phases.
Yanhui Wang, Susan V. Olesik
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Recent advances in the analysis of proteins have increased the demand for more efficient techniques to separate intact proteins. Enhanced-fluidity liquid chromatography (EFLC) involves the addition of liquefied CO2 to conventional liquid mobile phases.
Yanhui Wang, Susan V. Olesik
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Enhancing the characterization of intact proteins by ultraviolet photodissociation mass spectrometry
2022Access to high resolution mass spectrometers and high energy modes of activation such as electron- and photon-based modalities have enabled wider adoption of top-down methodologies, or strategies that allow the study of intact proteins. However, interpretation of MS/MS spectra of large proteins remains difficult owing to spectral congestion, charge ...
Dunham, Sean Duncan, 0000-0002-6214-7468
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Journal of Microbiological Methods, 2009
A method for biomarker candidate discovery and strain level pathogen characterization using liquid chromatography/mass spectrometry (LC/MS) with electrospray ionization is described. This method was applied to two pathogenic Clostridium species: C. difficile and C. perfringens.
Robert A, Everley +3 more
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A method for biomarker candidate discovery and strain level pathogen characterization using liquid chromatography/mass spectrometry (LC/MS) with electrospray ionization is described. This method was applied to two pathogenic Clostridium species: C. difficile and C. perfringens.
Robert A, Everley +3 more
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Global Quantification of Intact Proteins via Chemical Isotope Labeling and Mass Spectrometry
Journal of Proteome Research, 2019Although thousands of intact proteins have been feasibly identified in recent years, global quantification of intact proteins is still challenging. Herein, we develop a high-throughput strategy for global intact protein quantification based on chemical isotope labeling. The isotope incorporation efficiency is as high as 99.2% for complex intact protein
Zheyi Liu +4 more
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Processing Complex Mixtures of Intact Proteins for Direct Analysis by Mass Spectrometry
Analytical Chemistry, 2002For analysis of intact proteins by mass spectrometry (MS), a new twist to a two-dimensional approach to proteome fractionation employs an acid-labile detergent instead of sodium dodecyl sulfate during continuous-elution gel electrophoresis. Use of this acid-labile surfactant (ALS) facilitates subsequent reversed-phase liquid chromatography (RPLC) for a
Fanyu, Meng +5 more
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Analytical Chemistry, 2005
The characterization of protein glycosylation can be a complex and time-consuming procedure, especially for prokaryote O-linked glycoproteins, which often comprise unusual oligosaccharide structures with no known glycosylation motif. In this report, we describe a "top-down" approach that provides information on the extent of glycosylation, the ...
Schirm, M. +4 more
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The characterization of protein glycosylation can be a complex and time-consuming procedure, especially for prokaryote O-linked glycoproteins, which often comprise unusual oligosaccharide structures with no known glycosylation motif. In this report, we describe a "top-down" approach that provides information on the extent of glycosylation, the ...
Schirm, M. +4 more
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Development of mass spectrometry strategies for intact protein applications
Herein the use of high resolution Orbitrap mass spectrometry for accurate mass assignment and structural characterization of proteins is described. An advanced fragmentation method, ultraviolet photodissociation (UVPD), allowed assignment of structural features by generating numerous diagnostic ions.James, Virginia Kathryn +1 more
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Structural Characterization of Intact G Protein γ Subunits by Mass Spectrometry
2002Kevin L, Schey +4 more
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