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The Komives lab studies the biophysics of protein-protein interactions, particularly thrombin/thrombomodulin, the LDL-receptor-related protein and NF-kappaB/IkappaB. Binding kinetics are monitored by surface plasmon resonance, binding thermodynamics are measured by ITC, backbone dynamics are monitored by NMR and solvent accessibility is monitored by amide H/D exchange detected by MALDI-TOF mass spectrometry. The kinetic and thermodynamic experiments are complemented with site-directed mutagenesis to understand conformational changes and the role of individual amino acids in the interactions.

Track(s):
Molecular Pharmacology