The Callender Lab

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    SELECTED RECENT PUBLICATIONS

  • Difference FTIR Studies of Substrate Distribution in Triosephosphate Isomerase, H. Deng, J. Vedad, R. Z. B. Desamero and R. H. Callender, J. Phys. Chem B 121, 10036-10045 (2017). PMC5687254
  • Thermodynamic and structural adaptation differences between mesophilic and psychrophilic lactate dehydrogenases, S. Khrapunov, E. Chang and R. H. Callender, Biochemistry 56, 3587-3595 (2017). PMC5574168
  • Resolution of sub-millisecond kinetics of multiple reaction pathways for lactate dehydrogenase , M. Reddish, R. H. Callender and R. B. Dyer, Biophysical J. 112, 1852-1862 (2017). PMC5425397
  • The Dynamical Nature of Enzymatic Catalysis, R. Callender and R. B. Dyer, Accounts of Chemical Research 48, 407-413 (2015). PMC4333057
  • Mechanisms of Thermal Adaptation in the Lactate Dehydrogenases, H.-L. Peng, T. Egawa, E. Chang, H. Deng and R. H. Callender, J. Phys. Chem B 119, 15256-15262 (2015). PMC4679558
  • Energy Landscape of the Michaelis Complex of Lactate Dehydogenase: relationship to catalytic mechanism, Hua Deng, Ho-Lei Peng, Michael Reddish, R. Brian Dyer, Robert Callender, Biochemistry 53, 1849-1857 (2014). PMC3985751
  • Direct Evidence of Catalytic Heterogeneity in Lactate Dehydrogenase by Temperature Jump Infrared Spectroscopy, Michael Reddish”, Huo-Lei Peng, Hua Deng, Kunal Panwar, Robert Callender, R. Brian Dyer, J. Phys. Chem. B 118, 10854-10862 (2014). PMC4167064
  • On the Mechanism of Thermal Adaptation in the Lactate Dehydrogenases, Huo-Lei Peng, Tsuyoshi Egawa, Eric Chang, Hua Deng, Robert Callender, J. Phys. Chem. B 119, 15256-15262 (2015). PMC4679558
  • Large Scale Dynamics of the Michaelis Complex of B. Stearothermophilus Lactate Dehydrogenase revealed by Single Tryptophan Mutants Study, Nie, B., H. Deng, R. Desamero, and R. Callender. Biochemistry, 2013. 52: p. 1886-1892. PMC3604157
  • Investigation of Catalytic loop Structure, Dynamics, and Function Relationship of Yersina Protein Tyrosine Phosphatase by Temperature-Jump Relaxation Spectroscopy and X-ray Structural Determination, Ke, S., M.-C. Ho, N. Zhadin, H. Deng, and R. Callender. J. Phys. Chem B, 2012. 116: p. 6166-6176. PMC3380360
  • The Effect of Osmolytes on Protein Dynamics in the LDH-Catalyzed Reaction, Zhadin, N. and R. Callender. Biochemistry, 2011. 50: p. 1582-1589. PMC3075470
  • Conformational heterogeneity within the Michaelis complex of lactate dehydrogenase, Deng, H., D.V. Vu, K. Clinch, R. Desamero, R.B. Dyer, and R. Callender. J, Phys. Chem. B, 2011. 115: p. 7670-6778. PMC3111758
  • Pyrophosphate Activation in Hypoxanthine-Guanine Phosphoribosyltransferase with Transition State Analogue, Hua Deng, Robert Callender, Vern Schramm, and Charles Grubmeyer, Biochemistry 49, 2705-2714 (2010). PMC2851198
  • Loop-Tryptophan Human PNP Reveals Submillisecond Protein Dynamics, Mahmound Ghanem, Nickolay Zhadin, Robert Callender, and Vern L. Schramm, Biochemistry 48, 3658 (2009)
  • Probing the Role of Dynamics in Hydride Transfer Catalyzed by Lactate Dehydrogenase, Nickolay Zhadin, Miriam Gulotta, and Robert Callender", Biophysical J. 95, 1974-1984 (2008).
  • On the Pathway of Forming Enzymatically Productive Ligand-protein Complexes in Lactate Dehydrogenase, Hua Deng, Scott Brewer, Dung M. Vu, Keith Clinch, Robert Callender, and R. Brian Dyer, Biophysical J. 95, 804-813 (2008)
  • Lactate Dehydrogenase Undergoes a Substantial Structural Change to Bind its Substrate, Linlin Qiu, Miriam Gulotta, and Robert Callender, Biophysical J. 93, 1677-1686 (2007)
  • Ligand Binding and Protein Dynamics in Lactate Dehydrogenase, J. R. Exequiel T. Pineda, Robert Callender, and Steven D. Schwartz, Biophysical J. 93, 1474-1483 (2007)
  • Effects of Cell Volume Regulating Osmolytes on Glycerol-3-phosphate Binding to Triosphosphate Isomerase, Miriam Gulotta, Linlin Qiu, Jorg Rosgen, D. Wayne Bolen, and Robert Callender, Biochemistry 46, 10055-10062 (2007)
  • Loop Dynamics and ligand binding kinetics in the reaction catalyzed by the Yersinia protein tyrosine phosphatase, Mazdak Khajehpour, Li Wu, Sijiu Liu, Zhong-Yin Zhang, Nick Zhadin and Robert Callender, Biochemistry 46, 4370-4378 (2007)

    • SELECTED REVIEWS

  • The Dynamical Nature of Enzymatic Catalysis”, Robert Callender and R. Brian Dyer, Accounts of Chemical Research 48, 407-413 (2015). PMC4333057.
  • Time-Resolved Approaches to Characterize the Dynamical Nature of Enzyme Catalysis, Robert Callender and R. Brian Dyer, Chemical Reviews 106, 3031-3042 (2006). PMC16895316
  • Probing protein dynamics using temperature jump relaxation spectroscopy, R. Callender and R. B. Dyer, Curr Opin Struct Biol 12, 628-33 (2002)
  • Vibrational Studies of Enzymatic Catalysis, Hua Deng and Robert Callender, in Infrared and Raman Spectroscopy of Biological Materials, eds. Gremlich and Yan, pp. 477-515 (2001)
  • Raman spectroscopic studies of the structures, energetics, and bond distortions of substrates bound to enzymes, H. Deng and R. Callender, Methods Enzymol 308, 176-201 (1999)
  • Fast events in protein folding: the time evolution of primary processes, R. H. Callender, R. B. Dyer, R. Gilmanshin and W. H. Woodruff, Annu Rev Phys Chem 49, 173-202 (1998)
  • Infrared studies of fast events in protein folding, R. Brian Dyer, Feng Gai, William H. Woodruff, Rudolf Gilmanshin, and Robert Callender, Accs. Chem. Res. 31, 709-716 (1998)
  • Nonresonance Raman difference spectroscopy: a general probe of protein structure, ligand binding, enzymatic catalysis, and the structures of other biomacromolecules, R. Callender and H. Deng, Annu Rev Biophys Biomol Struct 23, 215-45 (1994)

    • Full List of Publications pdf