Biochemistry & Biophysics

Gregory D. Reinhart

reinhart Professor and Head, Biochemistry and Biophysics
Center for Advanced Biomolecular Research
Molecular Biophysics Training Program

Phone: (979) 862-2263
Email:gdr@tamu.edu
Visit the Reinhart lab Home Page
B.S. University of Illinois, Urbana (1973)
Ph.D. University of Wisconsin, Madison (1979)
Postdoc. Mayo Foundation (1979-1980)

Joined Texas A&M faculty in 1995

Molecular Basis of Enzyme Regulation
Our laboratory is interested in the mechanisms by which enzymes are regulated in the cell. In particular, we are interested in allosteric regulation of enzyme activity. Consequently, we are interested in understanding the nature of the conformational change in proteins that can be effected by the binding of ligands, and specifically how these changes alter the catalytic behavior of enzymes subject to allosteric regulation. We endeavor to investigate properties that are complementary to those determined by x-ray crystallography in order to develop a comprehensive picture of the structure-function relationships involved in the regulatory phenomenon. For example, we are interested in how the dynamics of protein structure might dictate the nature of an allosteric effect. Techniques and approaches that we use in the laboratory include analysis of enzyme kinetics; analysis of the thermodynamics of enzyme-ligand interactions; time-resolved and steady-state fluorescence spectroscopy; analysis of the effects of temperature and hydrostatic pressure (up to 4 kbar) on enzyme properties, site-specific mutagenesis, isothermal titration calorimetry, and molecular graphics.

Recent Publications
  1. Fenton AW & Reinhart GD (2009) Disentangling the Web of Allosteric Communication in a Homotetramer: Heterotropic Inhibition in Phosphofructokinase from Eschericia coli. Biochemistry
  2. Jung H, Yang T, Lasagna MD, Shi J, Reinhart GD & Cremer PS (2008) Impact of hapten presentation on antibody binding at lipid membrane interfaces. Biophys J 94: 3094-103
  3. Alston RW, Lasagna M, Grimsley GR, Scholtz JM, Reinhart GD & Pace CN (2008) Peptide sequence and conformation strongly influence tryptophan fluorescence. Biophys J 94: 2280-7
  4. Alston RW, Lasagna M, Grimsley GR, Scholtz JM, Reinhart GD & Pace CN (2008) Tryptophan fluorescence reveals the presence of long-range interactions in the denatured state of ribonuclease Sa. Biophys J 94: 2288-96
  5. Yu P, Lasagna M, Pawlyk AC, Reinhart GD & Pettigrew DW (2007) IIAGlc inhibition of glycerol kinase: a communications network tunes protein motions at the allosteric site. Biochemistry 46: 12355-65
  6. Johnson JL, West JK, Nelson AD & Reinhart GD (2007) Resolving the fluorescence response of Escherichia coli carbamoyl phosphate synthetase: mapping intra- and intersubunit conformational changes. Biochemistry 46: 387-97
  7. Quinlan RJ & Reinhart GD (2006) Effects of protein-ligand associations on the subunit interactions of phosphofructokinase from B. stearothermophilus. Biochemistry 45: 11333-41
  8. Sura GR, Lasagna M, Gawandi V, Reinhart GD & Fitzpatrick PF (2006) Effects of ligands on the mobility of an active-site loop in tyrosine hydroxylase as monitored by fluorescence anisotropy. Biochemistry 45: 9632-8
  9. Lovingshimer MR, Siegele D & Reinhart GD (2006) Construction of an inducible, pfkA and pfkB deficient strain of Escherichia coli for the expression and purification of phosphofructokinase from bacterial sources. Protein Expr Purif 46: 475-82
  10. Paricharttanakul NM, Ye S, Menefee AL, Javid-Majd F, Sacchettini JC & Reinhart GD (2005) Kinetic and structural characterization of phosphofructokinase from Lactobacillus bulgaricus. Biochemistry 44: 15280-6
  11. Quinlan RJ & Reinhart GD (2005) Baroresistant buffer mixtures for biochemical analyses. Anal Biochem 341: 69-76
  12. Riley-Lovingshimer MR & Reinhart GD (2005) Examination of MgATP binding in a tryptophan-shift mutant of phosphofructokinase from Bacillus stearothermophilus. Arch Biochem Biophys 436: 178-86
  13. Fenton AW, Paricharttanakul NM & Reinhart GD (2004) Disentangling the web of allosteric communication in a homotetramer: heterotropic activation in phosphofructokinase from Escherichia coli. Biochemistry 43: 14104-10
  14. Alston RW, Urbanikova L, Sevcik J, Lasagna M, Reinhart GD, Scholtz JM & Pace CN (2004) Contribution of single tryptophan residues to the fluorescence and stability of ribonuclease Sa. Biophys J 87: 4036-47
  15. Reinhart GD (2004) Quantitative analysis and interpretation of allosteric behavior. Methods Enzymol 380: 187-203
  16. Ortigosa AD, Kimmel JL & Reinhart GD (2004) Disentangling the web of allosteric communication in a homotetramer: heterotropic inhibition of phosphofructokinase from Bacillus stearothermophilus. Biochemistry 43: 577-86
  17. Fenton AW & Reinhart GD (2003) Mechanism of substrate inhibition in Escherichia coli phosphofructokinase. Biochemistry 42: 12676-81
  18. Pham AS & Reinhart GD (2003) Quantification of allosteric influence of Escherichia coli phosphofructokinase by frequency domain fluorescence. Biophys J 85: 656-66
  19. Fenton AW, Paricharttanakul NM & Reinhart GD (2003) Identification of substrate contact residues important for the allosteric regulation of phosphofructokinase from Eschericia coli. Biochemistry 42: 6453-9
  20. Fenton AW & Reinhart GD (2002) Isolation of a single activating allosteric interaction in phosphofructokinase from Escherichia coli. Biochemistry 41: 13410-6
Google