David E. Clemmer

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David E. Clemmer
David E Clemmer Image.png
Born (1965-02-23) February 23, 1965 (age 59)
Alma mater
Known for Ion mobility spectrometry, mass spectrometry
Awards Biemann Medal, ACS Chemical Instrumentation Award
Scientific career
Fields Analytical chemistry, mass spectrometry
Institutions Indiana University Bloomington
Doctoral advisor Peter B. Armentrout
Website www.indiana.edu/~clemmer/home.htm

David E. Clemmer (February 23, 1965, Alamosa, Colorado) is an analytical chemist and the Distinguished Professor and Robert and Marjorie Mann Chair of Chemistry at Indiana University in Bloomington, Indiana, where he leads the Clemmer Group. [1] Clemmer develops new scientific instruments for ion mobility mass spectrometry (IMS/MS), including the first instrument for nested ion-mobility time-of-flight mass spectrometry. [2] He has received a number of awards, including the Biemann Medal in 2006 "for his pioneering contributions to the integration of ion mobility separations with a variety of mass spectrometry technologies." [3]

Contents

Early life and education

Clemmer was born on February 23, 1965, to Ed Clemmer, an artist, and his wife MaryAnn, a teacher, of Alamosa, Colorado. [4] He attended Adams State College, where he originally majored in music, before changing to science. [4] He received his B.S. in chemistry with honors in 1987. He then attended the University of Utah, receiving his Ph.D. in physical chemistry in 1992. [5] His thesis advisor was Peter B. Armentrout, [2] with whom he studied transition metal ions in gaseous reactions. [3]

Career

During 1992–1993, Clemmer was a postdoctoral fellow in Japan, supported by the Japan Society for the Promotion of Science Fellowship at the Himeji Institute of Technology. He worked with Kenji Honma on electron transfer mechanisms [6] and reactions of excited-state metal atoms and gaseous molecules. [3] From 1993 to 1995, Clemmer was a postdoctoral research associate at Northwestern University, where he worked with Martin F. Jarrold, [3] studying protein folding and protein conformation in the gas phase, using techniques such as Ion-mobility spectrometry. [7] [8]

In 1995, Clemmer joined the Department of Chemistry at Indiana University. [3] He served as chair of the Chemistry Department from 2002 to 2006. [9] He is a full professor, and holds the Robert and Marjorie Mann Chair of Chemistry, to which he was named in 2002. [3] [5] He has published more than 230 papers. [1]

Among those who have influenced him, he includes Michael T. Bowers, Jesse L. Beauchamp, R. Graham Cooks, Scott A. McLuckey, Fred McLafferty, Evan R. Williams, Joseph A. Loo, Vicki Wysocki, and Julie A. Leary. [2] His graduate students have included Renã A. S. Robinson, Stephen Valentine, Cherokee Hoaglund-Hyzer, [10] and Catherine Srebalus Barnes. [11]

Research

Drift tube for ion mobility spectrometry Ion mobility spectrometry diagram.svg
Drift tube for ion mobility spectrometry

Clemmer is particularly interested in studying the structural characterization and conformational dynamics of complex low-symmetry systems. Clemmer develops scientific instruments and methods for the examination of biomolecular structure and complex biomolecular mixtures in the gas phase using ion-mobility spectrometry. [11]

Ion mobility methods separate ions into different groups based on their ability to move through an electrically-charged buffer gas. This enables complex mixtures to be differentiated in ways that could not be achieved by mass spectrometry alone. Even minute amounts of compounds can be distinguished and differentially examined according to characteristics such as size, shape and charge as well as mass. [2]

Clemmer has helped to establish ion mobility as both a powerful tool and a field of research through his "thorough studies" and "revolutionary instrumental methods". [3] In early work, Clemmer and Jarrold used long drift tubes with nonclustering gas atmospheres to increase the resolving power of ion-mobility spectrometry. [12] Clemmer's work on gas-phase separation methods for ion mobility-mass spectrometry (IM-MS) and their application to the structural analysis of intact proteins is considered a "particularly important milestone" in the application of IM-MS to the examination of biomolecular structures. [13] [14] [15] Clemmer and his colleagues have developed at least a dozen different configurations combining modular components for ion-mobility with mass spectrometry instruments. [2] [16] These include combining ion mobility with Time-of-flight mass spectrometry (TOF). [17] [18] [19] They also developed the first instrument for nested ion-mobility time-of-flight mass spectrometry. [2] [5]

Such equipment allows researchers to learn more about both the structures and the conformational dynamics of systems. [20] Clemmer has identified fundamental relationships between charge states and structures, and has shown that a single charge state can exist in more than one conformation in gaseous states. [3] Such techniques can be used for the study of both proteins and peptides. [21] [3] In early work, Clemmer showed that multiple conformations of the hemeprotein cytochrome c could be differentiated based on their mobilities. [22] In addition, the mobility of different chiral isomers was related to their protein folding. [23] More recent techniques enable researchers to track transitions in the conformations of macromolecular ions during the gas phase. A short pulse of ions is introduced into a drift tube by electrospray ionization. Structures separate based on differences in their mobilities. By exposing specific states to energizing collisions, new structures can be established and tracked through different conformational changes. Changes in conformation during the gas-phase data can then be mapped back to the original populations of structures. In this way, researchers can understand the possible pathways between structures. [24]

Understanding how protein folding occurs in three-dimensional molecules is one of biology's enduring problems. Proteins with different shapes often have very different biological activity and medical usefulness. [5] Clemmer's work has applications in the life sciences for understanding the conformation of structures in large protein complexes, [5] profiling the plasma proteome, [13] examining the role of proteins and protein folding in neurodegenerative diseases, [5] identifying possible cancer-related markers in blood, urine, or saliva, [4] and increasing the efficiency of drug-discovery. [25] Ion mobility-mass spectrometry techniques also allow the measurement and correlation of a wide variety of different characteristics simultaneously in a single analysis. Researchers can use these techniques to examine complex biological samples for lipidomics, proteomics, glycomics, and metabolomics information. [13]

Companies

Clemmer is a co-founder of Beyond Genomics, a systems biology company, and the founder of Predictive Physiology and Medicine, a biotechnology company specializing in personalized medicine. [4]

Hobbies

In addition to playing several instruments, Clemmer enjoys running marathons. [2]

Awards and honors

Related Research Articles

<span class="mw-page-title-main">Mass spectrometry</span> Analytical technique based on determining mass to charge ratio of ions

Mass spectrometry (MS) is an analytical technique that is used to measure the mass-to-charge ratio of ions. The results are presented as a mass spectrum, a plot of intensity as a function of the mass-to-charge ratio. Mass spectrometry is used in many different fields and is applied to pure samples as well as complex mixtures.

<span class="mw-page-title-main">Tandem mass spectrometry</span> Type of mass spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is a technique in instrumental analysis where two or more stages of analysis using one or more mass analyzer are performed with an additional reaction step in between these analyses to increase their abilities to analyse chemical samples. A common use of tandem MS is the analysis of biomolecules, such as proteins and peptides.

<span class="mw-page-title-main">Ion mobility spectrometry</span> Analytical technique used to separate and identify ionized molecules in the gas phase

Ion mobility spectrometry (IMS) It is a method of conducting analytical research that separates and identifies ionized molecules present in the gas phase based on the mobility of the molecules in a carrier buffer gas. Even though it is used extensively for military or security objectives, such as detecting drugs and explosives, the technology also has many applications in laboratory analysis, including studying small and big biomolecules. IMS instruments are extremely sensitive stand-alone devices, but are often coupled with mass spectrometry, gas chromatography or high-performance liquid chromatography in order to achieve a multi-dimensional separation. They come in various sizes, ranging from a few millimeters to several meters depending on the specific application, and are capable of operating under a broad range of conditions. IMS instruments such as microscale high-field asymmetric-waveform ion mobility spectrometry can be palm-portable for use in a range of applications including volatile organic compound (VOC) monitoring, biological sample analysis, medical diagnosis and food quality monitoring. Systems operated at higher pressure are often accompanied by elevated temperature, while lower pressure systems (1–20 hPa) do not require heating.

Hydrogen–deuterium exchange is a chemical reaction in which a covalently bonded hydrogen atom is replaced by a deuterium atom, or vice versa. It can be applied most easily to exchangeable protons and deuterons, where such a transformation occurs in the presence of a suitable deuterium source, without any catalyst. The use of acid, base or metal catalysts, coupled with conditions of increased temperature and pressure, can facilitate the exchange of non-exchangeable hydrogen atoms, so long as the substrate is robust to the conditions and reagents employed. This often results in perdeuteration: hydrogen-deuterium exchange of all non-exchangeable hydrogen atoms in a molecule.

A polyproline helix is a type of protein secondary structure which occurs in proteins comprising repeating proline residues. A left-handed polyproline II helix is formed when sequential residues all adopt (φ,ψ) backbone dihedral angles of roughly and have trans isomers of their peptide bonds. This PPII conformation is also common in proteins and polypeptides with other amino acids apart from proline. Similarly, a more compact right-handed polyproline I helix is formed when sequential residues all adopt (φ,ψ) backbone dihedral angles of roughly and have cis isomers of their peptide bonds. Of the twenty common naturally occurring amino acids, only proline is likely to adopt the cis isomer of the peptide bond, specifically the X-Pro peptide bond; steric and electronic factors heavily favor the trans isomer in most other peptide bonds. However, peptide bonds that replace proline with another N-substituted amino acid are also likely to adopt the cis isomer.

<span class="mw-page-title-main">Desorption electrospray ionization</span>

Desorption electrospray ionization (DESI) is an ambient ionization technique that can be coupled to mass spectrometry (MS) for chemical analysis of samples at atmospheric conditions. Coupled ionization sources-MS systems are popular in chemical analysis because the individual capabilities of various sources combined with different MS systems allow for chemical determinations of samples. DESI employs a fast-moving charged solvent stream, at an angle relative to the sample surface, to extract analytes from the surfaces and propel the secondary ions toward the mass analyzer. This tandem technique can be used to analyze forensics analyses, pharmaceuticals, plant tissues, fruits, intact biological tissues, enzyme-substrate complexes, metabolites and polymers. Therefore, DESI-MS may be applied in a wide variety of sectors including food and drug administration, pharmaceuticals, environmental monitoring, and biotechnology.

Robert Graham Cooks is the Henry Bohn Hass Distinguished Professor of Chemistry in the Aston Laboratories for Mass Spectrometry at Purdue University. He is an ISI Highly Cited Chemist, with over 1,000 publications and an H-index of 144.

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Michael L. Gross is Professor of Chemistry, Medicine, and Immunology, at Washington University in St. Louis. He was formerly Professor of Chemistry at the University of Nebraska-Lincoln from 1968–1994. He is recognized for his contributions to the field of mass spectrometry and ion chemistry. He is credited with the discovery of distonic ions, chemical species containing a radical and an ionic site on different atoms of the same molecule.

<span class="mw-page-title-main">Carol V. Robinson</span> British chemist and professor

Dame Carol Vivien Robinson, is a British chemist and former president of the Royal Society of Chemistry (2018–2020). She was a Royal Society Research Professor and is the Dr Lee's Professor of Physical and Theoretical Chemistry, and a professorial fellow at Exeter College, University of Oxford. She is the first director of the Kavli Institution for Nanoscience Discovery, University of Oxford, and she was previously professor of mass spectrometry at the chemistry department of the University of Cambridge.

<span class="mw-page-title-main">Ion-mobility spectrometry–mass spectrometry</span>

Ion mobility spectrometry–mass spectrometry (IMS-MS) is an analytical chemistry method that separates gas phase ions based on their interaction with a collision gas and their masses. In the first step, the ions are separated according to their mobility through a buffer gas on a millisecond timescale using an ion mobility spectrometer. The separated ions are then introduced into a mass analyzer in a second step where their mass-to-charge ratios can be determined on a microsecond timescale. The effective separation of analytes achieved with this method makes it widely applicable in the analysis of complex samples such as in proteomics and metabolomics.

Richard Dale Smith is a chemist and a Battelle Fellow and chief scientist within the biological sciences division, as well as the director of proteomics research at the Pacific Northwest National Laboratory (PNNL). Smith is also director of the NIH Proteomics Research Resource for Integrative Biology, an adjunct faculty member in the chemistry departments at Washington State University and the University of Utah, and an affiliate faculty member at the University of Idaho and the Department of Molecular Microbiology & Immunology, Oregon Health & Science University. He is the author or co-author of approximately 1100 peer-reviewed publications and has been awarded 70 US patents.

Renã A. S. Robinson is an associate professor and the Dorothy J. Wingfield Phillips Chancellor's Faculty Fellow in the department of chemistry at the Vanderbilt University, where she is the principal investigator of the RASR Laboratory.

Peter Nemes is a Hungarian-American chemist, who is active in the fields of bioanalytical chemistry, mass spectrometry, cell/developmental biology, neuroscience, and biochemistry.

Perdita Elizabeth Barran is a Professor of Mass Spectrometry at the University of Manchester. She is Director of the Michael Barber Centre for Collaborative Mass Spectrometry. She develops and applies ion-mobility spectrometry–mass spectrometry to the study of molecule structure and is searching for biomarkers for Parkinson's disease. She is Associate Dean for Research Facility Development at the University of Manchester. In 2020 and 2021 she was seconded to work for the Department of Health and Social Care as an advisor on the use case for mass spectrometry as a diagnostic method for diagnosis of COVID infection.

Martin F. Jarrold is a physical and analytical chemist known for contributions to ion-mobility spectrometry, heat capacity measurements of metal clusters, and charge detection mass spectrometry. Martin is the Robert & Marjorie Mann Chair in the Department of Chemistry at Indiana University.

<span class="mw-page-title-main">Claire E. Eyers</span> British biological mass spectrometrist

Claire Eyers is a British biological mass spectrometrist who is professor of biological mass spectrometry at the University of Liverpool, where she heads up the Centre for Proteome Research. Her research publications list her either as Claire E Haydon or Claire E Eyers.

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Erin Shammel Baker is an American bioanalytical chemist specializing in developing ion mobility-mass spectrometry hybrid instruments for biological and environmental applications. Baker is an expert in the research of perfluoroalkyl and polyfluoroalkyl substances analysis.

References

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