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Research in the Suo laboratory has three major directions:

1. Elucidate kinetic mechanisms of enzymes involved in DNA/RNA replication, repair, and lesion bypass
2. Understand Hepatitis C (HCV) replication and regulation of innate immunity
3. Develop antiviral and anticancer molecules based on rational drug design.

In the Suo lab, pre-steady state kinetic methods are employed using rapid chemical quench-flow and stopped-flow. These methods allow us to quench reactions on the millisecond time scale and to extract more kinetic information than the traditional steady-state kinetic methods. We also use protein engineering methods including site-directed mutagenesis and domain-swapping to study structure-function relationships of DNA polymerases. Recently, we have initiated projects to investigate the dynamics of a DNA polymerase using NMR and single-molecule techniques. X-ray crystallography will be used to examine interesting enzyme-substrate complexes. These multi-disciplinary approaches will allow us to develop new methods and to advance enzymology into unprecedented territory. Our goals are to understand the elementary steps of conformational changes and chemical reactions occurring at the active site of enzymes. Then, these mechanisms will be used for rational drug design. The designed enzyme inhibitors will be synthesized and tested in vitro and in vivo. Currently, we are investigating several systems described below.

(1) Pre-Steady State Kinetic Studies of DNA Lesion Bypass Polymerases

(2) Kinetic and Protein-Protein Interaction Studies of Human DNA Polymerases l, µ and TdT

(3) Design and Synthesis of Novel Nucleoside Analog Inhibitors

(4) Developing Anti-HCV Peptide-Based Inhibitors

(5) Effects of HCV Protease NS3/4A on Human Kinases Involved in Immune Response