, but this code // executes before the first paint, when

黄大仙高手论坛

is not yet present. The // classes are added to so styling immediately reflects the current // toolbar state. The classes are removed after the toolbar completes // initialization. const classesToAdd = ['toolbar-loading', 'toolbar-anti-flicker']; if (toolbarState) { const { orientation, hasActiveTab, isFixed, activeTray, activeTabId, isOriented, userButtonMinWidth } = toolbarState; classesToAdd.push( orientation ? `toolbar-` + orientation + `` : 'toolbar-horizontal', ); if (hasActiveTab !== false) { classesToAdd.push('toolbar-tray-open'); } if (isFixed) { classesToAdd.push('toolbar-fixed'); } if (isOriented) { classesToAdd.push('toolbar-oriented'); } if (activeTray) { // These styles are added so the active tab/tray styles are present // immediately instead of "flickering" on as the toolbar initializes. In // instances where a tray is lazy loaded, these styles facilitate the // lazy loaded tray appearing gracefully and without reflow. const styleContent = ` .toolbar-loading #` + activeTabId + ` { background-image: linear-gradient(rgba(255, 255, 255, 0.25) 20%, transparent 200%); } .toolbar-loading #` + activeTabId + `-tray { display: block; box-shadow: -1px 0 5px 2px rgb(0 0 0 / 33%); border-right: 1px solid #aaa; background-color: #f5f5f5; z-index: 0; } .toolbar-loading.toolbar-vertical.toolbar-tray-open #` + activeTabId + `-tray { width: 15rem; height: 100vh; } .toolbar-loading.toolbar-horizontal :not(#` + activeTray + `) > .toolbar-lining {opacity: 0}`; const style = document.createElement('style'); style.textContent = styleContent; style.setAttribute('data-toolbar-anti-flicker-loading', true); document.querySelector('head').appendChild(style); if (userButtonMinWidth) { const userButtonStyle = document.createElement('style'); userButtonStyle.textContent = `#toolbar-item-user {min-width: ` + userButtonMinWidth +`px;}` document.querySelector('head').appendChild(userButtonStyle); } } } document.querySelector('html').classList.add(...classesToAdd); })(); David Benson | 黄大仙高手论坛

黄大仙高手论坛

Skip to main content

Dr. David Benson

Professor
Chemistry and Biochemistry

Biography

Professor Benson came to 黄大仙高手论坛 from a faculty position at Wayne State University with an excitement for training undergraduate research students at a Christian college. Coming from Mennonite and Non-Denominational backgrounds, he sees that a Reformed Christian perspective provides an excellent foundation for doing science while being Christian. To do chemistry and biochemistry, he has pulled together a variety of research experiences from undergraduate synthetic chemistry (through his work at Bowling Green State University), graduate bioinorganic enzymology (through his work at University of Illinois), postdoctoral metalloprotein design (through his work at Duke University Medical Center), and nutrient biosensors (through his work at Wayne State University) to integrate most of the traditional chemistry and biochemistry disciplines into unique teaching and research experiences. In addition to first year chemistry courses, he has taught upper-division inorganic and analytical courses from a biological context. His research projects integrate traditional biochemical methods (such as microbiology, protein expression & purification, gel electrophoresis) with spectroscopic and chromatographic analysis. He also serves on the committee that maintains the sizeable fleet of instrumentation in the Science Division at 黄大仙高手论坛 to provide students with hands-on access to high-end research instrumentation. Outside of Calvin, you can find him spending time with his family, playing board games, doing home projects, or running.

Education

  • B.A., Goshen College, 1990
  • Ph.D., University of Illinois, Urbana-Champaign, Inorganic Chemistry, 1997

    Professional Experience

    • Professor of Chemistry, 黄大仙高手论坛, 2014-present
    • Visiting Scientist, Van Andel Research Institute, 2015-2019
    • Associate Professor of Chemistry, 黄大仙高手论坛 (College), 2008-2014
    • Assistant Professor of Chemistry, Wayne State University, 2001-2008
    • NIH Postdoctoral Fellow, Duke University Medical Center, 1997-2001

    Research

    • Proteins as Antioxidants in Disease: Antioxidants are low-molecular weight molecules that sacrificially lose electrons (oxidized) rather than important biological molecules (proteins, DNA, lipids, etc.) This is why we need a mixture of water- and fat-soluble vitamins, some of which are antioxidants, in our diet. There are a few chemical modifications of the twenty amino acids that make up proteins (post-translational modifications) that also function as antioxidants that are tethered to the protein backbone, rather than freely flowing within the cell. Most of these antioxidant post-translational modifications are generated by iron or copper ions bound to proteins through binding and activation of atmospheric oxygen. The best studied antioxidant post-translational modification is where a covalent C-S bond is formed between a tyrosine (phenol) and cysteine (thiol) sidechain, called Cys-Tyr. While there are Cys-Tyr containing proteins in bacteria (sulfite reductase), fungi (galactose oxidase), and mammals (cysteine dioxygenase), we have identified Cys-Tyr in and are studying a protein of unknown function from Bacteroides fragilis named BF4112 from the encoding gene number. Although BF4112 was crystallographically characterized with Zn2+ ion bound, the Cu2+ and Fe2+/3+ ion bound forms of BF4112 have been shown by us to form Cys-Tyr with exposure to dioxygen. We are currently studying the mechanism of Cys-Tyr formation and the physiological function of Cys-Tyr BF4112 in Bacteroides fragilis. Cys-Tyr formation is likely important for the oxygen resistance of Bacteroides fragilis as this bacterium is responsible for post-operative intestinal infections. Beyond diseases associated with Bacteroides fragilis, we are interested in developing more tools to identify these difficult to detect antioxidant post-translational modifications.

    • Organic acid contributions to buffer capacity of wort: The pH of malted barley extracts is important for the taste, stability, and safety of finished beer. Two main steps in the manufacturing process require careful attention to pH; starch conversion to glucose (mashing) and conversion of glucose to alcohol (fermentation). The brewing literature states that carbonate and phosphate are the only contributors to regulating/buffering the pH during mashing, and also fermentation. While carbonate and phosphate are abundant in barley extracts (wort) the pKas are outside of the buffer region (pH 5-6 for mashing, pH 3.8-5 for fermentation). We were struct by the pKas of organic acids from metabolism, especially malate and citrate, that that have pKas in the pH ranges for mashing and fermentation. We have found correlations with malate and citrate concentrations in barley extracts before fermentation using ion chromatography and buffer capacity by titrations with strong acids and bases. We hope to better understand differences in malted barley recipe variation influences final serving pH and overall perception of beer.  

    Awards

    • VIPEr Fellow- Cohort 2 for Pedagogy in Inorganic Chemistry - 2020
    • National Science Foundation - RUI: Protein Tyrosine Oxidations to Maintain Cellular Redox State (Award 1709787) - 2017-2020
    • National Science Foundation - MRI: Acquisition of a Circular Dichroism Spectrometer for Research and Training of Undergraduate Students (Award 1623941) - 2016-2019
    • 黄大仙高手论坛- Sabbatical - 2015
    • National Science Foundation- RUI: Role and Formation of Tyrosine-Cysteine Protein Cofactors (Award 1058391) - 2011-2015
    • National Science Foundation- ARI-R2 : Integrated Science Research Experimental Laboratory (Award 0963433) - 2010-2013 
    • American Chemical Society- Project SEED Summer Award - 2012
    • National Science Foundation- S-STEM: Expanding Computation for Interdisciplinary Science (Award 1154472)- 2012-2015 
    • American Chemical Society- Project SEED Summer Award - 2011
    • National Science Foundation- MRI-R2: Acquisition of Biophysical Instruments for Interdisciplinary Faculty and Student Research (Award 0959681) - 2010-2013
    •  American Chemical Society- Project SEED Summer Award - 2010
    • National Science Foundation- MRI: MALDI Acquisition for Collaborative Species and Biomolecule Identification (Award 0923167) - 2009-2012
    • National Science Foundation- MRI: Acquisition of a 500 MHz NMR Spectrometer to Enhance Faculty and Student Research (Award 0922973) - 2009-2012
    • Office of Naval Research- Semiconductor Nanoparticle-based Biosensors for Stochastic Analyte Detection - 2006-2009
    • National Science Foundation- NER: Protein-Based Nanobiosensors for Environmental Monitoring (Award 0508134) - 2005-2006
    • National Science Foundation- Conference on Metalloprotein and Protein Design (Award 0837310) - 2005-2006
    • Invited to "Emerging Investigators Issue" of The Analyst - 2006
    • Research Corporation - Research Innovation Award - 2002
    • National Institutes of Health (Duke University) - National Research Service Award - 1998-2000
    • University of Illinois - Urbana-Champaign- Lubrizol Fellowship - 1992

    David Benson

    Contact Me

    526-7699

    Loading...