# positions[].organizations[].parent[].label
College of Agriculture and Life Sciences

# overview
Our research interests lie in the interface between biology and other areas of science (chemistry and physics). NMR is our primary tool for structural and biophysical analysis. We also extensively use other techniques including Circular Dichroism and Fluorescence spectroscopy, and Isothermal calorimetry. These biophysical analyses are corroborated by sophisticated engineering and tuning of target proteins using semi-synthetic chemical biology techniques, in addition to traditional molecular biology methods.

# keywords[]
5 Development Of Treatments And Therapeutic Interventions

# educationAndTraining[].organization.label
Hanyang University - (Seoul, South Korea)

# educationAndTraining[].organization.label
Stony Brook University - (Stony Brook, New York, United States)

# educationAndTraining[].organization.label
Pohang University of Science and Technology - (Pohang, South Korea)

# publications[].label
Characterization of the Heparin Binding Site in the N-Terminus of Human Pro-Islet Amyloid Polypeptide: Implications for Amyloid Formation †

# publications[].label
The Unfolded State of NTL9 Is Compact in the Absence of Denaturant †

# publications[].label
Structure-guided design of a potent peptide inhibitor targeting the interaction between CRK and ABL kinase.

# publications[].label
Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing.

# publications[].label
Tuning protein autoinhibition by domain destabilization.

# publications[].label
Domain-Specific Incorporation of Noninvasive Optical Probes into Recombinant Proteins

# publications[].label
Experimental characterization of the denatured state ensemble of proteins.

# publications[].label
Temperature-dependent Hammond behavior in a protein-folding reaction: analysis of transition-state movement and ground-state effects.

# publications[].label
Entropy Hotspots for the Binding of Intrinsically Disordered Ligands to a Receptor Domain.

# publications[].label
Electrostatic interactions in the denatured state and in the transition state for protein folding: effects of denatured state interactions on the analysis of transition state structure.

# publications[].label
The structure and conformational plasticity of the nonstructural protein 1 of the 1918 influenza A virus.

# publications[].label
Kinetic Insights into the Binding between the nSH3 Domain of CrkII and Proline-Rich Motifs in cAbl.

# publications[].label
Thermodynamic contribution of backbone conformational entropy in the binding between SH3 domain and proline-rich motif.

# publications[].label
Ionic-Strength-Dependent Effects in Protein Folding: Analysis of Rate Equilibrium Free-Energy Relationships and Their Interpretation †

# publications[].label
Thermodynamics and kinetics of non-native interactions in protein folding: a single point mutant significantly stabilizes the N-terminal domain of L9 by modulating non-native interactions in the denatured state.

# publications[].label
Protein Side-Chain Dynamics and Residual Conformational Entropy

# publications[].label
Efficient high level expression of peptides and proteins as fusion proteins with the N-terminal domain of L9: application to the villin headpiece helical subdomain.

# publications[].label
Mutational analysis demonstrates that specific electrostatic interactions can play a key role in the denatured state ensemble of proteins.

# publications[].label
Mutational Analysis of the Folding Transition State of the C-Terminal Domain of Ribosomal Protein L9: A Protein with an Unusual β-Sheet Topology †

# publications[].label
Rational design, structural and thermodynamic characterization of a hyperstable variant of the villin headpiece helical subdomain.

# publications[].label
Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability.

# publications[].label
Denatured State Effects and the Origin of Nonclassical φ Values in Protein Folding

# publications[].label
ϕ-Value Analysis for Ultrafast Folding Proteins by NMR Relaxation Dispersion

# publications[].label
Molecular Mechanisms of Tight Binding through Fuzzy Interactions.

# publications[].label
Energetically significant networks of coupled interactions within an unfolded protein.

# publications[].publisher
Proceedings of the National Academy of Sciences

# publications[].label
The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State.

# publications[].label
Solution Structure and Folding Characteristics of the C-Terminal SH3 Domain of c-Crk-II † , ‡

# publications[].label
Side chain dynamics of carboxyl and carbonyl groups in the catalytic function of Escherichia coli ribonuclease H.

# publications[].label
Analysis of the pH-dependent folding and stability of histidine point mutants allows characterization of the denatured state and transition state for protein folding.

# publications[].label
Binding Mechanism of the N-Terminal SH3 Domain of CrkII and Proline-Rich Motifs in cAbl.

# publications[].label
The Molecular Mechanisms Underlying the Hijack of Host Proteins by the 1918 Spanish Influenza Virus.

# researcherOn[].label
Structure and functional dynamics of virus-host protein interactions

# researcherOn[].awardedBy.label
National Institutes of Health - (Bethesda, Maryland, United States)

# researcherOn[].awardedBy.preferredLabel
DHHS-NIH-National Institute of General Medical Science

# researcherOn[].label
Molecular mechanisms whereby a pandemic influenza A virus antagonizes host antiviral immune responses

# researcherOn[].awardedBy.label
National Institute of Food and Agriculture - (Washington D.C., District of Columbia, United States)

# streetAddress
Texas A&M University; Biochemistry & Biophysics; 2128 TAMU

# schools[]
College of Agriculture and Life Sciences