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Topic: Thermal ionization mass spectrometry methods and applications in the earth and ocean sciences Overview by Prof. Elizabeth Griffith, School of Earth Sciences, OSU Application by Ms. Samantha Carter, Griffith Research Group, OSU Date: September 24 Time: 5:30 PM Place: JAMES B050 (460 W. 10TH Ave)

Please join us for the 3rd Annual Ohio Mass Spectrometry and Metabolomics Symposium (OMSMS) to be held at the Blackwell Inn and Pfahl Conference Center at The Ohio State University in Columbus, Ohio, on October 1-2, 2019. Invited keynote and plenary presentations: Connecting the World’s Mass Spectrometry Data to Understand the Chemistry of Life — a Big […]

“Panoptic Mass Spectrometry: How and Why” Date: Sept 16, 2019 Time: 4:10 PM Place: 130 CBEC

Protein function depends critically on intrinsic internal dynamics, which is manifested in distinct ways, such as loop motions that regulate protein recognition and catalysis. Under physiological conditions, dynamic processes occur on a wide range of time scales from subpicoseconds to seconds. Commonly used NMR spin relaxation in solution provides valuable information on very fast and slow motions but is insensitive to the intermediate nanosecond to microsecond range that exceeds the protein...

Protein function depends critically on intrinsic internal dynamics, which is manifested in distinct ways, such as loop motions that regulate protein recognition and catalysis. Under physiological conditions, dynamic processes occur on a wide range of time scales from subpicoseconds to seconds. Commonly used NMR spin relaxation in solution provides valuable information on very fast and slow motions but is insensitive to the intermediate nanosecond to microsecond range that exceeds the protein...

Mr. Taghi Sahraeian, Badu Research Group, OSU “Droplet Imbibition Enables Non-Equilibrium Interfacial Reactions in Charged Microdroplets” Date: August 27th Time: 5:30 PM Place: 105 BRT COH-MSDG – Central Ohio (OH) Mass Spectrometry Discussion Group

Mowei Zhou will present a seminar while visiting us from Pacific Northwest National Laboratory next week: “Deciphering Proteins with Unknown Functions in Plants using Top-Down and Native Mass Spectrometry Techniques” Tuesday, August 20, 2019 4:00 pm BRT 105 Mass spectrometry (MS) has been widely used in proteomics applications for identifying and quantifying proteins in biological […]

Oral cancer is a public health problem with an incidence of almost 50,000 and a mortality of 10,000 each year in the USA alone. Black raspberries (BRBs) have been shown to inhibit oral carcinogenesis in several preclinical models, but our understanding of how BRB phytochemicals affect the metabolic pathways during oral carcinogenesis remains incomplete. We used a well-established rat oral cancer model to determine potential metabolic pathways impacted by BRBs during oral carcinogenesis. F344...

Oral cancer is a public health problem with an incidence of almost 50,000 and a mortality of 10,000 each year in the USA alone. Black raspberries (BRBs) have been shown to inhibit oral carcinogenesis in several preclinical models, but our understanding of how BRB phytochemicals affect the metabolic pathways during oral carcinogenesis remains incomplete. We used a well-established rat oral cancer model to determine potential metabolic pathways impacted by BRBs during oral carcinogenesis. F344...

A special seminar will be presented by Dr. Michael T. Marty (University of Arizona) on Uncovering Antimicrobial Peptide Interactions in Lipid Nanodiscs by Native MS. Tuesday, June 25th 10:00-11:00 am BRT 105 Research in the Marty lab is focused on developing mass spectrometry methods to study the structure and biophysics of membrane proteins. Working at […]

Related Articles

Structural analysis of phospholipase A2 from functional perspective. 1. Functionally relevant solution structure and roles of the hydrogen-bonding network.

Biochemistry. 1999 Mar 09;38(10):2909-18

Authors: Yuan C, Byeon IJ, Li Y, Tsai MD

Abstract
Bovine pancreatic phospholipase A2 (PLA2), a small (13.8 kDa) Ca2+-dependent lipolytic enzyme, is rich in functional and structural character. In an effort to examine its detailed structure-function relationship, we determined its solution structure by multidimensional nuclear magnetic resonance (NMR) spectroscopy at a functionally relevant pH. An ensemble of 20 structures generated has an average root-mean-square deviation (RMSD) of 0.62 +/- 0.08 A for backbone (N, Calpha, C) atoms and 0.98 +/- 0.09 A for all heavy atoms. The overall structure shows several notable differences from the crystal structure: the first three residues at the N-terminus, the calcium-binding loop (Y25-T36), and the surface loop (V63-N72) appear to be flexible; the alpha-helical conformation of helix B (E17-F22) is absent; helix D appears to be shorter (D59-V63 instead of D59-D66); and the hydrogen-bonding network is less defined. These differences were analyzed in relation to the function of PLA2. We then further examined the H-bonding network, because its functional role or even its existence in solution has been in dispute recently. Our results show that part of the H-bonding network (the portion away from N-terminus) clearly exists in solution, as evidenced by direct observation (at 11.1 ppm) of a strong H-bond between Y73 and D99 and an implicated interaction between D99 and H48. Analyses of a series of mutants indicated that the existence of the Y73.D99 H-bond correlates directly with the conformational stability of the mutant. Loss of this H-bond results in a loss of 2-3 kcal/mol in the conformational stability of PLA2. The unequivocal identification and demonstration of the structural importance of a specific hydrogen bond, and the magnitude of its contribution to conformational stability, are uncommon to the best of our knowledge. Our results also suggest that, while the D99.H48 catalytic diad is the key catalytic machinery of PLA2, it also helps to maintain conformational integrity.

PMID: 10074343 [PubMed - indexed for MEDLINE]

We will have an off-semester seminar presented by Prof. Eugene Nikolaev (Skoltech Institute of Science and Technology, Moscow, Russia) on “The importance of isotopic fine structures in ultrahigh resolution FT-ICR analyses”. Prof. Nikolaev is a well-known and prominent scientist who has made significant contribution to Fourier-transform Ion Cyclotron Resonance (FT-ICR) mass spectrometry analyses and instrument […]

1. Mr. Ben Burris, Badu Research Group, OSU “Probing Kinetics of Biomolecular Reactions via Contained-ESI Mass Spectrometry” 2. Ms. Maddy Lomax-Vogt, Olesik Research Group, OSU “Inductively Coupled Plasma Fundamentals and Nanoparticle Measurements” Date: April 23 Time: 5:30 PM Place: 2015 MP

Prof. Jenny Brodbelt, Department of Chemistry, The University of Texas at Austin “Lipid analysis using UVPD” Date: March 25 Time: 5:30 PM Place: BRT 115

Machine learning is now being increasingly employed in radiology to assist with tasks such as automatic lesion detection, segmentation, and characterisation. We are currently involved in an National Institute of Health Research (NIHR)-funded project, which aims to develop machine learning methods to improve the diagnostic performance and reduce the radiology reading time of whole-body magnetic resonance imaging (MRI) scans, in patients being staged for cancer (MALIBO study). We describe here the...

1. Prof. Chris Zhu, Human Sciences, OSU “Studies of gut bacterial metabolites using MS-based metabolomics and an in vitro human colonic model (HCM)” 2. Dr. Djawed Bennouna, Kopec Research Group, OSU “The Study of the impact of environment and genetics on the nutritional quality of rapeseed by a metabolomic approach” Date: February 26 Time: 5:30 […]

Ms. Devin Swiner, Badu Research Group, Ohio State “Microsampling with Cotton Threads” Dr. Dalton Snyder, CCIC, Ohio State “Neutral loss MS/MS scans in a linear quadrupole ion trap and application to analysis of pharmaceutical mixtures via ion/molecule reactions” Date: January 22nd Time: 5:30PM Location: TBA

Metabolomics aims at the comprehensive identification of metabolites in complex mixtures to characterize the state of a biological system and elucidate their roles in biochemical pathways. For many biological samples, a large number of spectral features observed by NMR spectroscopy and mass spectrometry (MS) belong to unknowns, i.e., these features do not belong to metabolites that have been previously identified, and their spectral information is not available in databases. By combining NMR,...

Metabolomics aims at the comprehensive identification of metabolites in complex mixtures to characterize the state of a biological system and elucidate their roles in biochemical pathways. For many biological samples, a large number of spectral features observed by NMR spectroscopy and mass spectrometry (MS) belong to unknowns, i.e., these features do not belong to metabolites that have been previously identified, and their spectral information is not available in databases. By combining NMR,...

Dr. Arpad Somogyi, CCIC, Ohio State “Availability of a new ion mobility technique TIMS (trapped ion mobility spectrometry), in the CCIC Mass Spec and Proteomics Facility: implementation on a Q-TOF and an FT-ICR instrument ” Prof. Abraham Badu-Tawiah, Badu Research Group, Ohio State “New Approaches for Ultra-small Volume Analysis by Mass Spectrometry” Date: December 4th […]