A new instrument configuration based on a Finnigan FTMS-2000 platform has been applied to the study of surface-induced dissociation (SID) in this research. Benzene monomer ions C(6)H(6)(+) and dimer ions (C(6)H(6))(2)(+) were impacted on a fluorinated self-assembled monolayer surface at collision energies ranging from 1 to 70 eV. Benzene cations were chosen for this study because the fragmentation characteristics of the molecular cation are well known and its SID has been thoroughly investigated. SID spectra obtained by FTMS-SID are very similar to those reported in the literature for the same surface but exhibit much higher mass resolution. A comparison study of collision-induced dissociation (CID) and SID of benzene molecular cations was performed utilizing the same ICR cell and ion detection protocol. It is demonstrated that SID provides both much higher energy deposition and a narrower internal energy distribution than CID. The present instrument geometry and experimental protocol demonstrate much higher efficiencies than previous SID studies by FTMS and much higher mass resolution than previous SID studies using other types of mass analyzers.
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http://dx.doi.org/10.1021/ac9612887 | DOI Listing |
J Int Soc Prev Community Dent
October 2024
Department of Basic Dental Science, College of Dentistry, University of Mosul, Mosul, Iraq.
Aim: To evaluate the micro-shear bond strength (µ-SBS) of resin-modified glass ionomer cement and to assess the chemical and topographical changes in the zirconia fitting surface induced by acidulated phosphate fluoride (APF) gel using scanning electron microscope (SEM) analysis and Fourier transform infrared (FTIR) spectroscopy.
Materials And Methods: Thirty-two samples were prepared from two zirconia materials, UPCERA HT White and BruxZir Solid Zirconia, milled by a computer-aided design/computer-aided manufacturing system. From each zirconia sample, six plates were prepared for FTIR and SEM testing.
J Am Soc Mass Spectrom
January 2025
Native MS Guided Structural Biology Center, The Ohio State University, Columbus, Ohio 43210, United States.
Anal Chem
December 2024
Department of Chemistry and Applied Biosciences, ETH Zurich, Zurich CH-8093, Switzerland.
Solution and gas-phase measurements can provide valuable insights into biomolecular conformational dynamics. By comparing the data from such experiments, it is possible to elucidate the nature of the interactions governing a biomolecule's stability. Here, we measured human, bovine, and porcine hemoglobin stability in solution and the gas phase using collision-induced dissociation, collision-induced unfolding, surface-induced dissociation, and temperature-controlled nanoelectrospray mass spectrometry.
View Article and Find Full Text PDFACS Cent Sci
August 2024
Native Mass Spectrometry Guided Structural Biology Center, Ohio State University, Columbus, Ohio 43210, United States.
We illustrate the utility of native mass spectrometry (nMS) combined with a fast, tunable gas-phase charge reduction, electron capture charge reduction (ECCR), for the characterization of protein complex topology and glycoprotein heterogeneity. ECCR efficiently reduces the charge states of tetradecameric GroEL, illustrating Orbitrap / measurements to greater than 100,000 /. For pentameric C-reactive protein and tetradecameric GroEL, our novel device combining ECCR with surface induced dissociation (SID) reduces the charge states and yields more topologically informative fragmentation.
View Article and Find Full Text PDFSe Pu
July 2024
CAS Key Laboratory of Separation Sciences for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China.
Dynamic changes in the structures and interactions of proteins are closely correlated with their biological functions. However, the precise detection and analysis of these molecules are challenging. Native mass spectrometry (nMS) introduces proteins or protein complexes into the gas phase by electrospray ionization, and then performs MS analysis under near-physiological conditions that preserve the folded state of proteins and their complexes in solution.
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