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Investigators and Program Directors

Griselda Hernández

Griselda Hernández

Research Scientist, Wadsworth Center,
Computational & Structural Biology Adjunct Assistant Professor, School of Public Health, Biomedical Sciences

Ph.D., University of Rochester (1991)
Postdoctoral training, University of California at Davis, Los Alamos National Laboratory

E-mail: griselda@wadsworth.org

<< Research Interests

Select Publications

Publications 2004 to present:

  • LeMaster, D.M., Anderson, J.S., and Hernández, G. (2009). Peptide Conformer Acidity Analysis of Protein Flexibility Monitored by Hydrogen Exchange. Biochemistry, 48, 9256-9265.
  • Hernández, G., Anderson, J.S., and LeMaster, D.M. (2009). Polarization and Polarizability Assessed by Protein Amide Acidity. Biochemistry, 48, 6482-6494.
  • Anderson, J.S., Hernández, G., and LeMaster, D.M. (2009). Backbone Conformational Dependence of Peptide Acidity. Biophys. Chem. 141:124-130.
  • Anderson, J.S., Hernández, G., and LeMaster, D.M. (2008). A Billion-fold Range in Acidity for the Solvent-Exposed Amides of Pyrococcus furiosus Rubredoxin. Biochemistry, 47:6178-6188.
  • Hernández, G., Anderson, J.S., and LeMaster, D.M. (2008). Electrostatic Stabilization and General Base Catalysis in the Active Site of the Human Protein Disulfide Isomerase a Domain Monitored by Hydrogen Exchange. ChemBioChem, 9:768-778.
  • LeMaster, D.M., Anderson, J.S., Wang, L., Guo, Y., Li, H., and Hernández, G. (2007). NMR and X-ray Analysis of Structural Additivity in Metal Binding Site-Swapped Hybrids of Rubredoxin. BMC Struct. Biol., 7, 81.
  • LeMaster, D.M., Anderson, J.S., and Hernández, G. (2007). Spatial Distribution of Dielectric Shielding in the Interior of Pyrococcus furiosus Rubredoxin as Sampled in the Subnanosecond Timeframe by Hydrogen Exchange. Biophys. Chem., 129:43-48.
  • LeMaster, D.M., Anderson, J.S., and Hernández, G. (2007). Normal Carbon Acid Referencing for Protein Amide Hydrogen Exchange. Magn. Res. Chem., 45:601-604.
  • LeMaster, D.M., and Hernández, G. (2007). Residue Cluster Additivity of Thermodynamic Stability in the Hydrophobic Core of Mesophile vs. Hyperthermophile Rubredoxins. Biophys. Chem. 2007, 125:483-489.
  • Anderson, J.S., LeMaster, D.M., Hernández, G. (2006). Electrostatic Potential Energy within a Protein Monitored by Metal Charge-Dependent Hydrogen Exchange. Biophys. J., 2006, 91, L93-L95.
  • LeMaster, M., Hernández, G. (2006). Additivity of Differential Conformational Dynamics in Hyperthermophile/Mesophile Rubredoxin Chimeras as Monitored by HydrogenExchange. ChemBioChem, 7:1886-1889.
  • LeMaster, D.M., Minnich, M., Parsons, P.J., Anderson, J.S., Hernández, G. (2006). Tetrathiolate Coordination of Germanium (IV) in a Protein Active Site. J. Inorg. Biochem. 100:1410-1412.
  • LeMaster, D.M., Anderson, J.S., Hernández, G. (2006). Role of Native-State Structure in Rubredoxin Native-State Hydrogen Exchange. Biochemistry 45:9956-9963.
  • LeMaster, D.M., Tang, J., Paredes, D.I., Hernández, G. (2005). Enhanced Thermal Stability Achieved without Increased Conformational Rigidity at Physiological Temperatures: Spatial Propagation of Differential Flexibility in Rubredoxin Hybrids. Proteins 61:608-616.
  • LeMaster DM, Hernández G. (2005). Additivity in both Thermodynamic Stability and Thermal Transition Temperature for Rubredoxin Chimeras via Hybrid Native Partitioning. Structure 13:1153-1163.
  • LeMaster, D.M., Hernández, G. (2005). Hybrid Native Partitioning of Interactions among Nonconserved Residues in Chimeric Proteins. Proteins 60:723-731.
  • LeMaster, D.M., Tang, J.Z., Paredes, D.I., Hernández, G. (2005). Contribution of the multi-turn Segment in the Reversible Thermal Stability of Hyperthermophile Rubredoxin: NMR Thermal Chemical Exchange Analysis of Sequence Hybrids. Biophys. Chem. 116:57-65.
  • LeMaster, D.M., Tang, J.Z., Hernández, G. (2004). Absence of Kinetic Thermal Stabilization in a Hyperthermophile Rubredoxin Indicated by 40 Microsecond folding in the Presence of Irreversible Denaturation. Proteins 57:118-127.
  • Tang, J.Z., Hernández, G., LeMaster, D.M. (2004). Increased Peptide Deformylase Activity for N-formylmethionine Processing of Proteins Overexpressed in Escherichia Coli: Application to Homogeneous Rubredoxin Production. Protein Expres. Purif. 36:100-105.

Invited book chapter:

  • Hernández, G. and LeMaster, D.M. NMR Analysis of Native-State Protein Conformational Flexibility by Hydrogen Exchange, Methods in Molecular Biology, 2009, vol. 490:285-310,  Protein Structure, Stability and Interactions ed. Shriver, J.W. (Humana Press).
  • Anderson, J.S., Hernández, G. and LeMaster, D.M., Conformational Electrostatics in the Stabilization of the Peptide Anion. Current Organic Chemistry, in press.
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Contact Information

Phone: (518) 474-4673
FAX: (518) 473-2900
E-mail: griselda@wadsworth.org