Project description:This dataset contains native mass spectrometry data for the purified AflR-DBD (DNA-binding domain) protein. The experiment was performed to determine the accurate molecular mass of the protein using native electrospray ionization conditions. The protein was analyzed in 150 mM ammonium acetate buffer using a Q Exactive UHMR mass spectrometer with nanoESI ionization.
Project description:This project includes raw data for protein posttranslational acetylation analysis, native mass analysis, and TOF-MS analysis of SmaATase
Project description:Native mass spectrometry (MS) involves the analysis and characterization of macromolecules, predominantly intact proteins and protein complexes, whereby as much as possible the native structural features of the analytes are retained. As such, native MS enables the study of secondary, tertiary, and even quaternary structure of proteins and other biomolecules. Native MS represents a relatively recent addition to the analytical toolbox of mass spectrometry and has over the past decade experienced immense growth, especially in enhancing sensitivity and resolving power but also in ease of use. With the advent of dedicated mass analyzers, sample preparation and separation approaches, targeted fragmentation techniques, and software solutions, the number of practitioners and novel applications has risen in both academia and industry. This review focuses on recent developments, particularly in high-resolution native MS, describing applications in the structural analysis of protein assemblies, proteoform profiling of─among others─biopharmaceuticals and plasma proteins, and quantitative and qualitative analysis of protein-ligand interactions, with the latter covering lipid, drug, and carbohydrate molecules, to name a few.
Project description:To investigate the impact of Toxoplasma gondii GRA35 on neuronal cells and the underlying mechanisms, we conducted GST-pull down experiments to isolate proteins that bind to GRA35-GST and GST in neuronal cells, respectively. The dataset labeled "20240706_WJ_ GRA35_N_B01.raw" corresponds to the GRA35-GST group, whereas "20240706_WJ_C1_B01.raw" represents the data for the GST group. Subsequent mass spectrometry analysis revealed that the neuron-specifically expressed RTN1c protein interacts with GRA35.
Project description:Electrothermal supercharging of protein ions formed by electrospray ionization from buffered aqueous solutions results in significant increases to both the maximum and average charge states compared to native mass spectrometry in which ions are formed from the same solutions but with lower spray potentials. For eight of the nine proteins investigated, the maximum charge states of protonated ions formed from native solutions with electrothermal supercharging is greater than those obtained from conventional denaturing solutions consisting of water/methanol/acid, although the average charging is slightly lower owing to contributions of small populations of more folded low charge-state structures. Under these conditions, electrothermal supercharging is slightly less effective for anions than for cations. Equivalent sequence coverage (80%) is obtained with electron transfer dissociation of the same high charge-state ion of cytochrome c formed by electrothermal supercharging from native solutions and from denaturing solutions. Electrothermal supercharging should be advantageous for combining structural studies of proteins in native environments with mass spectrometers that have limited high m/z capabilities and for significantly improving tandem mass spectrometry performance for protein ions formed from solutions in which the molecules have native structures and activities.