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Femtobiology, Biomolecular Interactions, Protein Dynamics Research in the Zhong group is directed towards understanding the nature of elementary processes in biological systems. We relate dynamics and structures to functions at the most fundamental level with state-of-the-art femtosecond lasers and molecular biology techniques. The laboratory ultimately will have the capability of time resolution from femtosecond to millisecond (second); biological systems can be prepared and studied at the single molecule level. We are currently focusing on studies of molecular recognition and ultrafast protein/enzyme dynamics of several important biological systems. |
Biomolecular recognition is governed by physical forces and the understanding of electrostatic interactions at the atomic scale is fundamental to protein science. Here, we are particularly interested in protein-DNA/ligand binding processes and study local hydration, complex rigidity and conformation dynamics. Intrinsic amino acid residue tryptophan has been characterized in various biological environments to probe electrostatic interactions; several important resonance energy transfer pairs have been developed to study conformational changes. Molecular mutation is used to investigate site-specific interactions. These studies are very important to drug transport and design, protein folding and unfolding, and enzyme catalysis. |
A variety of ultrafast elementary reactions involved in protein functioning such as twist motion, proton, electron and energy transfer, and bond breaking and making will be studied. Site-direct mutagenesis will be used to alter structurally and chemically important residue(s) to study the local reactivity. These studies will elucidate the role of dynamics in structure-dynamics-function correlation and the nature of non-equilibrium biological dynamics by coherent femtosecond laser preparation. Currently, we focus on DNA-repair enzymes (photolyases) to map out the entire evolution of functional processes and thus reveal the molecular mechanism of this important biological function. A similar photosensory protein (cryptochrome) is also being studied to elucidate its key photochemistry for synchronization of biological timing (circadian rhythm). |