University of Nebraska-Lincoln
Lincoln, NE 68588-0304
For more information vist http://chemweb.unl.edu/dsmith/
Mass spectrometry has been an important part of nearly all of my approximately 180 publications. In the earliest stage of my research career (years 1965-1975), I designed and constructed specialized mass spectrometers for studies of gas phase ion-molecule reactions. Drs. Jean Futrell and Marvin Vestal, two widely recognized leaders in the field of mass spectrometry fundamentals, were mentors during this period. In the next stage of my research career (years 1976-1984), my interest shifted to applications of mass spectrometry to identify modified forms of nucleic acids. During this time, I developed high sensitivity methods for exact mass measurements, chemical derivatization, advanced instrumentation for field desorption ionization, and GC MS interfaces optimized for highly polar compounds. Dr. James McCloskey, the leader in this area, was my mentor.
In 1984, I took my first tenure-track position (Purdue University) where I developed several research programs based on applications of mass spectrometry for analysis of biomaterials. Major areas include structure elucidation of proteins and natural products, development of stable isotope tracer methodology for calcium and magnesium, and initial development of methods for studying the folded structures of proteins. Many of the protein structure studies focused on the causes of cataract and involved proteins isolated from the eye lens. During this period I was also Director of the Purdue University School of Pharmacy Mass Spectrometry Laboratory.
In 1994, I was appointed Director of the Nebraska Center for Mass Spectrometry where research on the causes of cataract, the folded structures of proteins and calcium tracer methods continued. Areas of greatest emphasis include protein folding, protein-protein interactions, the structures of large complexes (e.g., chaperonins and viral particles) and proteomics.
Selected Publications(1) Down-sizing improves sensitivity 100-fold for hydrogen exchange-mass spectrometry. L. Wang; D.L. Smith, Anal. Biochem. 314 46-53 (2003).
(2) Mass spectrometric quantification of acetylation at specific lysines within the amino terminal tail of histone H4. C.M. Smith; P.R. Gafken; Z. Zhang; D.E. Gottschling; J.B. Smith; D.L. Smith, Anal. Biochem. 316 23-33 (2003).
(3) Rate and equilibrium constants for protein unfolding and refolding determined by hydrogen exchange-mass spectrometry. Y. Deng; D.L. Smith, Anal. Biochem. 276 150-160 (1999).
(4) Identification and localization of slow, natural, cooperative unfolding in the Hck SH2 domain by amide hydrogen exchange and mass spectrometry. J.R. Engen; T.E. Smithgall; W.H. Gmeiner; D.L. Smith, Biochemistry 36 14384-14391 (1997).
(5) Determination of Amide Hydrogen Exchange by Mass Spectrometry: A New Tool for Protein Structure Elucidation.Z. Zhang; D.L. Smith, Protein Science 2, 522-531, (1993).
(6) Determination of Benzo(a)pyrene Sulfate Conjugates from Benzo(a)pyrene-Treated Cells by Continuous-Flow Fast Atom Bombardment Mass Spectrometry. Y. Teffera; W.M. Baird; D.L. Smith, Anal. Chem. 63, 453-456, (1991).
(7) Elucidation of the Primary Structures of Proteins by Mass Spectrometry. J.B. Smith; G. Thevenon, D.L. Smith; B. Green, Anal. Biochem. 193, 118-124, (1991).
(8) Absorption of Calcium and Magnesium from Fortified Human Milk by Very Low Birthweight Infants. Y.M. Liu; P. Neal; J. Ernst; C. Weaver; K. Rickard; D.L. Smith; J. Lemons, Pediatr. Res. 25, 496-502 (1989).
(9) Internal Energy Effects and Collisional Energy Transfer in the Reaction of D3+ with CH4. D.L. Smith; J.H. Futrell, J. Phys. B: Atomic and Mol. Phys. 8, 803 (1975).
(10) Dissociative Charge Exchange of Rare-Gas Ions with C2F6 and C3F8. D.L. Smith and L. Kevan, J. Chem. Phys. 46, 1586 (1967).