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Dmitry Korzh

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Last Updated: 02 July 2021

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Dmitry Korzh

Full nameDmitriy Mihaylowic Korj
Date of birth( 1971-10-29 ) 29 October 1971 (age 49)
Place of birthTurkmen SSR , Soviet Union
Height1.82 m (6 ft 0 in)
Playing position(s)Defender
FacebookDmitry-Korzh

The primary focus of my laboratory is studies of protein structure, dynamics and interactions using structural biology methods, including nuclear magnetic resonance spectroscopy and X-ray crystallography. We make use of cutting-edge TROSY-NMR techniques that allow us to access structural dynamics and interactions of protein assemblies with molecular weights of up to 1 MDa, opening an avenue for deciphering molecular mechanisms of their action. The underlying cause of cancer is spontaneous mutations introduced to genomic DNA. Reactive products of cellular metabolism and external genotoxic agents cause persistent DNA damage, which is constantly removed through various DNA repair mechanisms. It is unavoidable, however, that some DNA modifications persist into S-phase, creating blocks for progression of DNA replication machinery. To circumvent this problem, organisms in all kingdoms of life have evolved DNA damage tolerance pathways, employing specialized enzymes that bypass DNA lesions while temporarily leaving DNA damage unrepaired. The vast majority of mutations are introduced in the genome by enzymes of error-prone branch of DNA damage tolerance-translesion DNA synthesis. Genetic changes that ensue as result of TLS are at the root of the onset of cancer and development of various resistance mechanisms displayed by relapsed tumors, which represent a major problem for treatment of some types of cancer, including ovarian and lung. Our research is aimed at obtaining a detailed atomic-resolution picture of structure, dynamics and interactions of proteins and protein assemblies involved in DNA damage tolerance pathways that will aid development of new strategies for cancer therapy. Intermediate and transition states of biomolecular processes represent paradigm of functionally important structure in biology. For example, protein self-assembly involves formation of partially folded and misfolded protein state prone to aggregation implicated in a number of human disorders, including type-II diabetes, Alzheimer's and Parkinson's diseases. Although characterization of such species can provide vital clues about mechanisms of underlying processes, it is extremely challenging to examine such states because they are populated at low levels and are not readily isolate. One of the research directions in my laboratory is studies of intermediate and transition states of protein folding and binding using novel NMR relaxation dispersion methodology.

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