Mass spectrometry across the sciences

McLafferty, Fred W.

doi:10.1073/pnas.0800784105

Cited by 24 publications

(21 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Mass spectrometry (MS) has undergone dramatic evolution in two decades ranging from routine analysis of small molecules to challenging measurements of mega-dalton protein assemblies [1, 2]. To keep large protein assemblies or complexes nearly intact, native ESI can be employed to introduce them to the gas phase.…”

Section: Introductionmentioning

confidence: 99%

Native electrospray ionization and electron-capture dissociation for comparison of protein structure in solution and the gas phase

Zhang

Cui

Gross

2013

International Journal of Mass Spectrometry

View full text Add to dashboard Cite

The importance of protein and protein-complex structure motivates improvements in speed and sensitivity of structure determination in the gas phase and comparison with that in solution or solid state. An opportunity for the gas phase measurement is mass spectrometry (MS) combined with native electrospray ionization (ESI), which delivers large proteins and protein complexes in their near-native states to the gas phase. In this communication, we describe the combination of native ESI, electron-capture dissociation (ECD), and top-down MS for exploring the structures of ubiquitin and cytochrome c in the gas phase and their relation to those in the solid-state and solution. We probe structure by comparing the protein's flexible regions, as predicted by the B-factor in X-ray crystallography, with the ECD fragments. The underlying hypothesis is that maintenance of structure gives fragments that can be predicted from B-factors. This strategy may be applicable in general when X-ray structures are available and extendable to the study of intrinsically disordered proteins.

show abstract

Section: Introductionmentioning

confidence: 99%

Native electrospray ionization and electron-capture dissociation for comparison of protein structure in solution and the gas phase

Zhang

Cui

Gross

2013

International Journal of Mass Spectrometry

View full text Add to dashboard Cite

show abstract

“…Mass spectrometry (MS) is a powerful tool for identification and characterization of chemicals with high specificity and sensitivity . The development of atmospheric pressure ionization techniques, such as electrospray ionization (ESI) and atmospheric pressure chemical ionization (APCI), has significantly widened the applications of MS analysis and enabled the coupling of liquid chromatography with MS.…”

Section: Introductionmentioning

confidence: 99%

Gas‐flow assisted ion transfer for mass spectrometry

Garimella

Huang

et al. 2012

J. Mass. Spectrom.

View full text Add to dashboard Cite

Methods and devices that use gas flows to collect ions and transfer them over long distances for mass spectrometric analysis have been developed. Gas flows derived from the ionization source itself or provided by means of additional pumping were used to generate a laminar flow inside cylindrical tube. Hydrodynamic simulations and experimental tests demonstrate that laminar flow can transfer ions over long distance. The typical angular discrimination effects encountered when sampling ions from ambient ionization sources are minimized, and the sampling of relatively large surface areas is demonstrated with desorption electrospray ionization (DESI). Ion transfer over 6 m has been achieved and its application to multiplexed chemical analysis is demonstrated on samples at locations remote from the mass spectrometer.

show abstract

“…Mass spectrometry is a powerful tool for the identification of proteins and the characterization of variable protein posttranslational modifications (PTMs) 21-26. Electrospray ionization mass spectrometry has played an important role in the analysis of PTMs, and with additional HPLC, is capable of measuring the mass of macromolecules with high accuracy 22, 27, 28.…”

Section: Introductionmentioning

confidence: 99%

Identification of Novel Protein Kinase A Phosphorylation Sites in the M-domain of Human and Murine Cardiac Myosin Binding Protein-C Using Mass Spectrometry Analysis

et al. 2010

View full text Add to dashboard Cite

Cardiac myosin binding protein-C (cMyBP-C) is a large multi-domain accessory protein bound to myosin thick filaments in striated muscle sarcomeres. It plays an important role in the regulation of muscle contraction and mutations in the gene encoding cMyBP-C are a common cause of familial hypertrophic cardiomyopathy, the leading cause of sudden cardiac death in young people 1 . The N-terminal domains including the C0, C1, cMyBP-C motif, and C2 domains play a crucial role in maintaining and modulating actomyosin interactions (keeping normal cardiac function) in a phosphorylation dependent manner. The cMyBP-C motif or "M-domain" is a highly conserved linker domain in the N-terminus of cMyBP-C that contains three to five protein kinase A (PKA) phosphorylation sites, depending on species. For the human isoform, three PKA sites were previously identified (Ser 275 , Ser 284 , and Ser 304 ), while three homologous sites exist in the murine isoform (Ser 273 , Ser 282 , and Ser 302 ). The murine cMyBP-C isoform contains an additional conserved consensus site, Ser 307 that is not present in the human isoform. In this study, we investigated sites of PKA phosphorylation of murine and human cMyBP-C by treating the recombinant protein C0C2 (~50 KDa, which contains the N-terminal C0, C1, M, and C2 domains) and C1C2 (~35 KDa, contains C1, M and C2 domains) with PKA and assessing the phosphorylation states using SDS-PAGE with ProQ Diamond staining, and powerful hybrid mass spectrometric analyses. Both high-accuracy bottom-up and measurements of intact proteins mass spectrometric approaches were used to determine the phosphorylation states of C0C2 and C1C2 proteins with or without PKA treatment. Herein, we report for the first time that there are four PKA phosphorylation sites in both murine and human M-domains; both murine Ser 307 and a novel * To whom correspondence should be addressed. Prof. Julie A. Leary, Ph.D., Dept. of Molecular and Cellular Biology, U.C. Davis, 130 Briggs Hall, 1 Shields Rd, Davis,; jaleary@ucdavis.edu. § Both authors contributed equally to this work. Supporting Information Available:Supplementary materials containing more detailed technical information of methods, sequence information of proteins, schematic diagram of various species of cMyBP-C M-domains, more MS 2 and MS 3 spectra of identified phosphorylation sites, and more mass spectra of intact proteins. This material is available free of charge via the Internet at

show abstract

Mass spectrometry across the sciences

Cited by 24 publications

References 12 publications

Native electrospray ionization and electron-capture dissociation for comparison of protein structure in solution and the gas phase

Native electrospray ionization and electron-capture dissociation for comparison of protein structure in solution and the gas phase

Gas‐flow assisted ion transfer for mass spectrometry

Identification of Novel Protein Kinase A Phosphorylation Sites in the M-domain of Human and Murine Cardiac Myosin Binding Protein-C Using Mass Spectrometry Analysis

Contact Info

Product

Resources

About