David N. M. Jones, Ph.D.
Assistant Professor of Pharmacology
Department of Pharmacology
University of Colorado at Denver and Health Sciences Center
RC1 South Tower, Room 6116
P.O. Box 6508 MS 8303
Aurora, Colorado 80045
Phone: 303.724-3601
David.Jones@uchsc.edu
EDUCATION/EXPERIENCE
Research Interests:
The use of NMR Spectroscopy to Probe the Relationship Between
Protein Structure and Disease
I am interested in understanding
how the three-dimensional structure of proteins and nucleic acids controls their
biological function. Changes in the chemical composition of a protein, perhaps
through a spontaneous mutation can disrupt its structure which may dramatically
interfere with its normal function. This in turn can lead to the development of
diseases such as cancer. Understanding the fine balance between structure and
function and how these correlate with the onset of disease is one of the major
challenges for pharmacologists and biochemists today. If we can find out how the
structure of a molecule defines its biological function we can begin to design
new pharmaceutical drugs for fighting disease. Research in my lab uses Nuclear
Magnetic Resonance (NMR) spectroscopy to study the structure and dynmaics of biological
molecules implicated in the development and progression of disease. NMR spectroscopy
is used to solve the three dimensional structures of molecules in solution. However
this is only the first step in understanding structure-function relationships
in proteins. NMR is one of the only techniques that can provide information about
how flexibility of a protein contributes to its function. As an example, many
proteins change their structure on binding to a drug or other ligand. Understanding
the dynamics was an important part of the design of HIV protease inhibitors for
the treatment of AIDS patients. My laboratory uses NMR to probe the contributions
that dynamic processes make to understanding the function of proteins.
Selected Publications
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L.K. Dow, Jones, D.N.M., Wolfe, S.A., Verdine, G.L.,
and Churchill, M.E.A. Structural Studies of the High Mobility
Group Globular Domain and Basic Tail of HMG-D Bound to Disulfide
Cross-linked DNA. Biochemistry, (2000), 39(32): p. 9725-9736.
[Abstract]
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Jones, D.N.M. and Bendiak, B. Novel multi-dimensional
heteronuclear NMR techniques for the study of 13C-O-acetylated
oligosaccharides: expanding the dimensions for carbohydrate
structures. J. Biomol. NMR, (1999), 15: p. 157-168. [Abstract]
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Wang, B., Jones, D.N.M., Kaine, B.P., and Weiss, M.A.,
High-resolution structure of an archaeal zinc ribbon defines
a general architectural motif in eukaryotic RNA polymerases.
Structure, (1998), 6(5): p. 555-569. [Abstract]
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Burkoth, T.S., Benzinger, T.L.S., Jones, D.N.M., Hallenga, K., Meredith,
S.C., and Lynn, D.G. C-terminal PEG blocks the irreversible step in beta-amyloid(10-
35) fibrillogenesis. J. Amer. Chem. Soc., (1998), 120(30): p. 7655-7656. (Communication)
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Benzinger, T.L.S., Braddock, D.T., Dominguez, S.R., Burkoth,
T.S., Miller-Auer, H., Subramanian, R.M., Fless, G.M., Jones,
D.N.M., Lynn, D.G., and Meredith, S.C. Structure-function
relationships in side chain lactam cross- linked peptide models
of a conserved N-terminal domain of apolipoprotein E. Biochemistry,
(1998), 37(38): p. 13222-13229. [Abstract]
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Fletcher, C.M., Jones, D.N.M., Diamond, R., and Neuhaus, D. Treatment
of NOE constraints involving equivalent or nonstereoassigned protons in calculations
of biomacromolecular structures. J. Biomol. NMR, (1996), 8(3): p. 292-310. [Abstract]
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Churchill, M.E.A., Jones, D.N.M., Glaser, T., Hefner,
H., Searles, M.A., and Travers, A.A. HMG-D Is an Architecture-Specific
Protein That Preferentially Binds to DNA Containing the Dinucleotide
TG. EMBO Journal, (1995), 14(6): p. 1264-1275. [Abstract]
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Jones, D.N.M., Searles, M.A., Shaw, G.L., Churchill,
M.E.A., Ner, S.S., Keeler, J., Travers, A.A., and Neuhaus, D.
The Solution Structure and Dynamics of the DNA-Binding Domain
of HMG-D From Drosophila melanogaster. Structure, (1994), 2(7):
p. 609-627. [Abstract]
Bibliography
Primary
website for Dr. Jones
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