Ming Dong Research Lab at UNCW
Ming Dong Research Lab at UNCW
Protein-Protein interactions with regulations
There are numerous phosphorylation-dependent signaling pathways which are modulated by redox signaling. We work on structures of the phosphorylated proteins, kinase-substrate complexes and redox-modified proteins to have an in-depth understanding of their interaction mechanisms involved in the signaling pathways.
Transaminase and its other roles
We apply biochemistry, X-ray crystallography and computational modeling to obtain a deep understanding of the relationship of protein structure and function with an emphasis on redox regulated phosphorylated enzymes involved in cell signaling.
Protein Conformational Sampling
We are interested in the subtle protein conformational changes (sampling) which can be crucial for the catalysis process. Protein conformational sampling can be in various modes which are linked to various activation energies. With ambient temperature crystallography we are able to observe alternate conformational changes of side chains of amino acids which will provide a better understanding of how networks of residue conformational motions work in a high vs low efficiency sampling mode. A better understanding of the relationship between structure, dynamics, and function, will inform us how to best modulate a protein’s function.
As we know, PFAS can be pretty bad
These super tough man-made molecules can bind to proteins in our body and sometimes occupy the binding sites that were designed by nature to bind with their substrates. We developed tools to uncover their binding partners from human proteins and further learn their binding mechanisms.