Charles G. Hoogstraten
Assistant Professor
- B.S. 1990, Michigan State University, Chemistry & Biochemistry
- Howard Hughes Medical Institute Predoctoral Fellowship, 1990-1995
- Ph.D. 1995, University of Wisconsin - Madison
- Helen Hay Whitney Postdoctoral Fellow, 1995-1998, University of Colorado, Boulder
- Visiting Postdoctoral Fellow/Junior Research Specialist, 1998-2002, UC Davis, Chemistry
hoogstr3@msu.edu
302D Biochemistry Building
Michigan State University
East Lansing, MI 48824-1319
Office: 517-353-3978
FAX: 517-353-9334
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Charles G. Hoogstraten
Research Interests
One major area of interest is the study of the relationships between
conformational dynamics, metal ion cofactors, and the catalytic mechanisms
of catalytic RNA molecules (ribozymes). Solution-state NMR is unparalleled
in its ability to give comprehensive site-specific information on the
extent and timescales of dynamics of internal motions in macromolecules.
We are interested in novel schemes to use this information to pick apart
theconformational transitions that are a key part of the reaction coordinate
for many ribozymes. Comparisons of NMR data with kinetic studies of ribozyme
variants, or "dynamics-function" studies, provide particular
insight into mechanism. As polyanions, catalytic RNA molecules often require
divalent metal cation cofactors, which can play either structural or functional
roles. We complement the NMR studies by using pulsed EPR to determine
the structure of such metal ion sites in ribozymes and other RNA molecules. MORE Hoogstraten, C.G. & Johnson, J.E., Jr. (2008) Metabolic Labeling: Taking advantage of bacterial pathways to prepare spectroscopically useful isotope patterns in proteins and nucleic acids. Concepts Magn. Reson. Ser. A 32, 34-55. Hoogstraten CG, Sumita M. (2007) Structure-function relationships in RNA and RNP enzymes: Recent advances. Biopolymers. 87:317-328. Vogt M, Lahiri S, Hoogstraten CG, Britt RD, DeRose
VJ. (2006) Coordination environment of a site-bound metal ion in the
hammerhead ribozyme determined by 15N and 2H ESEEM spectroscopy.
J Am Chem Soc. 27;128(51):16764-70. Johnson JE Jr, Julien KR, Hoogstraten CG. (2006) Alternate-site isotopic labeling of ribonucleotides for NMR
studies of ribose conformational dynamics in RNA.
J Biomol NMR. 35(4):261-74. Hoogstraten, C.G., Grant, C.V., & Britt, R.D. (2002) Water counting: Quantitating the Hydration Level of Metal Ions Bound to Nucleotides and Nucleic Acids. RNA 8, 252-260. 
The Hoogstraten
laboratory studies biologically and biochemically important problems using
techniques derived from biophysics and physical chemistry. Specifically,
we are interested in the structure and function of RNA as studied using
high-resolution nuclear magnetic resonance spectroscopy (NMR) in the liquid
state, contemporary electron paramagnetic resonance (EPR) spectroscopy,
and other techniques including solution thermodynamics.
Recent Publications
Hoogstraten, C.G., Grant, C.V., Horton, T.E., DeRose, V.J., & Britt, R.D. (2002) Structural Analysis of Metal Ion Ligation to Nucleotides and Nucleic Acids Using Pulsed EPR Spectroscopy. J. Am. Chem. Soc. 124, 834-842.
Summers, J.S., Hoogstraten, C.G., Britt, R.D., Base, K., Shaw, B.R., Ribeiro, A.A., & Crumbliss, A.L. (2001) 31P NMR Probes of Chemical Dynamics: Paramagnetic Relaxation Enhancement of the 1H and 31P NMR Resonances of Methylphosphite and Methylethylphosphate Anions by Selected Metal Complexes. Inorg. Chem. 40, 6547-6554.
Hoogstraten, C.G., Wank, J.R., & Pardi, A. (2000) Active Site Dynamics in the Lead-Dependent Ribozyme. Biochemistry 39, 9951-9958.MORE