Photo of Dmitry M. Korzhnev, Ph.D.

Dmitry M. Korzhnev, Ph.D.

Assistant Professor, Department of Molecular Biology and Biophysics
Academic Office Location:
Molecular Biology and Biophysics
UConn Health
263 Farmington Avenue
Farmington, CT 06030-3305
Phone: 860-679-2849
Fax: 860-679-3408

Molecular Biology & Biochemistry Graduate Program

M.S.Moscow Institute of Physics and Technology Applied Physics and Mathematics
Ph.D.Moscow Institute of Physics and Technology Biophysics

Post-Graduate Training
PostdoctoralSwedish NMR Centre at Göteborg UniversityPost-Doctoral Fellow in Structural Biology in Swedish NMR Centre at Göteborg University under supervision of Prof. M. Billeter
PostdoctoralShemyakin-Ovchinnikov Inst. Bioorganic ChemistryResearch training in Structural Biology under supervision of Prof. A.S. Arseniev
PostdoctoralUniversity of TorontoPost-Doctoral Fellow in Structural Biology (NMR) under supervision of Prof. L.E. Kay

Name of Award/HonorAwarding Organization
Post-doctoral Fellowship 2003-2004Canadian Institutes of Health Research (CIHR)
Post-doctoral Fellowship 2003-2005(CIHR) Training Program in Protein Folding
Post-doctoral Fellowship Wenner-Gren Foundation
Russian State Fellowship for Outstanding Young Scientists Russian Academy of Sciences
Anniversary Moscow Region Governor Grant for Young Scientists Moscow Region Government
Ph.D. Fellowships 1996-1998International Soros Science Education Program
M.S. Fellowship International Soros Science Education Program
Name & DescriptionCategoryRoleTypeScopeStart YearEnd Year
Connecticut NMR Workshop 2014: Data processing and analysis for protein structure and dynamicsWorkshop/ConferenceCo-chairExternalRegional20142014
Graduate Admissions CommitteeEducation CommitteeMemberUConn HealthUniversity2012
NESS 2012 - The 9th Annual North Eastern Structure Symposium on Protein Dynamics: From Folding to FunctionWorkshop/ConferenceChair ExternalRegional20122012
Connecticut NMR Workshop 2012: Data processing and analysis for protein structure and dynamicsWorkshop/ConferenceCo-ChairExternalRegional20122012
Graduate Admissions CommitteeEducation CommitteeMemberUConn HealthUniversity20112011
PhD dissertation committee - Mr. Janus Vang Education CommitteeMemberUConn HealthUniversity20112012
PhD dissertation committee - Mr. Matthew Fenwick Education CommitteeMemberUConn HealthUniversity2010

The primary focus of my laboratory is studies of protein structure, dynamics and interactions using structural biology methods, including nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography. We make use of cutting-edge TROSY-NMR techniques that allow 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 (lesions) persist into S-phase, creating blocks for progression of the 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 (TLS). Genetic changes that ensue as a result of TLS are at the root of the onset of cancer and the development of various resistance mechanisms displayed by relapsed tumors, which represents 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 the development of new strategies for cancer therapy.

Intermediate and transition states of biomolecular processes represent a paradigm of functionally important structure in biology. For example, protein self-assembly involves the formation of partially folded and misfolded protein states prone to aggregation implicated in a number of human disorders, including type-II diabetes, Alzheimer's and Parkinson's diseases. Although the characterization of such species can provide vital clues about the mechanisms of the underlying processes, it is extremely challenging to examine such states because they are populated at low levels and are not readily isolated. 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.

Accepting students for Lab Rotations: Summer '17, Fall '17, Spring '18

Lab Rotation Projects
- Structure, dynamics and interactions of proteins involved in DNA damage tolerance pathways
- Studying folding mechanisms of single-domain proteins. Structure determination of folding intermediates

Journal Articles

Book Chapters

  • NMR study of bacteriorhodopsin structure and dynamics
    Arseniev, A.S., Korzhnev, D.M., Orekhov, V.Yu., Maslennikov, I.V. Protein Structures: Kaleidoscope of Structural Properties and Functions 2003 Jan;273-297