{"id":266,"date":"2017-08-17T22:11:43","date_gmt":"2017-08-18T02:11:43","guid":{"rendered":"https:\/\/health.uconn.edu\/bezsonova-lab\/?page_id=266"},"modified":"2026-06-06T17:09:08","modified_gmt":"2026-06-06T21:09:08","slug":"dmitry-korzhnev","status":"publish","type":"page","link":"https:\/\/health.uconn.edu\/bezsonova-lab\/dmitry-korzhnev\/","title":{"rendered":"Dmitry Korzhnev’s Lab"},"content":{"rendered":"
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  • \"\"<\/li>\n <\/ul>\n <\/div>\n \n <\/div>\n<\/div><\/div><\/div><\/div>

    Research<\/h3>

    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.<\/p>\n

    DNA damage tolerance and cancer:<\/strong><\/p>\n

    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.<\/p>\n

    Protein folding and dynamics:<\/strong><\/p>\n

    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.<\/p>\n<\/div><\/div><\/div>

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    • \"\"
      REV1 C-terminal Domain<\/div><\/div><\/li>\n
    • \"\"
      SHPRH PHD Domain<\/div><\/div><\/li>\n
    • \"\"
      REV1 BRCT Domain<\/div><\/div><\/li>\n
    • \"\"
      Rad18 UBZ Domain in Complex with Ubiquitin <\/div><\/div><\/li>\n <\/ul>\n <\/div>\n \n <\/div>\n<\/div><\/div><\/div><\/div>

      Publications<\/h3>\t\t\t

      2026<\/h2>\n

      USP1 inhibition promotes RAD18-dependent PCNA degradation and BRCA1 synthetic lethality<\/strong>
      Ashton NW, Ravindranathan R, Korchak EJ, Somuncu OS, Zambrano GA, Mukkavalli SV, Asada S, Korzhnev DM, Bezsonova I, D\u2019Andrea AD.
      bioRxiv. 2026 May 10:2026.02.25.708068.
      doi: 10.64898\/2026.02.25.708068
      PMID: 42146504 (preprint)<\/p>\n

      \n

      2025<\/h2>\n

      Long-range destabilizing effects of mutations at the Escherichia coli \u03b2 clamp dimer interface<\/strong>
      Liriano ML, Berger MB, Nguyen K, Korzhnev DM, Cisneros GA, Beuning PJ.
      Biochemistry. 2025 Jul 15;64(14):3126\u20133136.
      doi: 10.1021\/acs.biochem.5c00135
      PMID: 40574562<\/p>\n

      Functional asymmetry in processivity clamp proteins<\/strong>
      Mahdi S, Beuning PJ, Korzhnev DM.
      Biophys J. 2025 May 20;124(10):1549\u20131561.
      doi: 10.1016\/j.bpj.2025.04.014
      PMID: 40247618<\/p>\n

      Activation dynamics of ubiquitin-specific protease 7<\/strong>
      Valles GJ, Korchak EJ, Geddes-Buehre DH, Jaiswal N, Korzhnev DM, Bezsonova I.
      PNAS. 2025 May 27;122(21):e2426632122.
      doi: 10.1073\/pnas.2426632122
      PMID: 40397674<\/p>\n

      Divide-and-conquer strategy for NMR studies of the E. coli \u03b3-clamp loader complex<\/strong>
      Mahdi S, Semenova IV, Bezsonova I, Beuning PJ, Korzhnev DM.
      J Biomol NMR. 2025;79(4):243\u2013257.
      doi: 10.1007\/s10858-025-00471-0
      PMID: 40694188<\/p>\n

      Differences in structure, dynamics, and zinc coordination between isoforms of human ubiquitin ligase UBE3A<\/strong>
      Bregnard TA, Fairchild D, Chen X, Erlandsen H, Tarasov SG, Walters KJ, Korzhnev DM, Bezsonova I.
      J Biol Chem. 2025 Feb;301(2):108149.
      doi: 10.1016\/j.jbc.2024.108149
      PMID: 39742997<\/p>\n

      REV1 inhibition enhances trinucleotide repeat mutagenesis<\/strong>
      Siegel A, Almstead D, Kothandaraman N, Reich J, Lamkin E, Victor JA, Grover A, Ikeh K, Koval H, Crompton A, Jang H, Lee H, Del Rio Guerra R, Korzhnev DM, Hadden MK, Hong J, Zhou P, Chatterjee N.
      bioRxiv. 2025 Sep 16:2025.09.11.675234.
      doi: 10.1101\/2025.09.11.675234
      PMID: 41000971 (preprint)<\/p>\n

      REV1 inhibition enhances trinucleotide repeat mutagenesis<\/strong>
      Siegel A, Almstead D, Kothandaraman N, Reich J, Lamkin E, Victor J, Grover A, Ikeh K, Koval H, Crompton A, Jang H, Lee H, Del Rio-Guerra R, Korzhnev D, Hadden MK, Hong J, Zhou P, Chatterjee N.
      Open Biol. 2025 Dec 1;15(12):250234.
      doi: 10.1098\/rsob.250234
      PMID: 41537824<\/p>\n

      \n

      2024<\/h2>\n

      Probing hot spots of protein-protein interactions mediated by the safety-belt region of REV7<\/strong>
      Dash RC, Arianna GA, Patel SM, Rizzo AA, Harrahill NJ, Korzhnev DM, Hadden MK.
      Structure. 2024 Nov 7;32(11):2134\u20132146.e3.
      doi: 10.1016\/j.str.2024.09.007
      PMID: 39366370<\/p>\n

      Backbone NMR resonance assignments of stabilized E. coli \u03b2 clamp<\/strong>
      Mahdi S, Lim S, Bezsonova I, Beuning PJ, Korzhnev DM.
      Biomol NMR Assign. 2024;18(2):293\u2013297.
      doi: 10.1007\/s12104-024-10202-5
      PMID: 39269602<\/p>\n

      Protein assemblies in translesion synthesis<\/strong>
      Arianna GA, Korzhnev DM.
      Genes (Basel). 2024;15(7):832.
      doi: 10.3390\/genes15070832
      PMID: 39062611<\/p>\n

      Lead compound profiling for small molecule inhibitors of REV1-CT\/RIR interaction<\/strong>
      Zaino AM, Dash RC, James SJ, MacGilvary N, Crompton A, McPherson KS, Stanzione M, Korzhnev DM, Dyson NJ, Chatterjee N, Cantor SB, Hadden MK.
      Bioorg Med Chem. 2024 May 15;106:117755.
      doi: 10.1016\/j.bmc.2024.117755
      PMID: 38749343<\/p>\n

      Effects of xylanase A double mutation on substrate specificity and structural dynamics<\/strong>
      MacDonald ME, Wells NGM, Hassan BA, Dudley JA, Walters KJ, Korzhnev DM, Aramini JM, Smith CA.
      J Struct Biol. 2024 Jun;216(2):108082.
      doi: 10.1016\/j.jsb.2024.108082
      PMID: 38438058<\/p>\n

      \n

      2023<\/h2>\n

      Conformational exchange at a C2H2 zinc-binding site facilitates redox sensing by PML protein<\/strong>
      Bregnard TA, Fairchild D, Erlandsen H, Semenova IV, Szczepaniak R, Ahmed A, Weller SK, Korzhnev DM, Bezsonova I.
      Structure. 2023 Sep 7;31(9):1086\u20131099.e6.
      doi: 10.1016\/j.str.2023.06.014
      PMID: 37473756<\/p>\n

      Backbone and ILV methyl NMR assignments of Rev7\/Rev3 complexes<\/strong>
      Arianna GA, Geddes-Buehre DH, Korzhnev DM.
      Biomol NMR Assign. 2023 Jun;17(1):107\u2013114.
      doi: 10.1007\/s12104-023-10128-4
      PMID: 37129702<\/p>\n

      Activation Dynamics of Ubiquitin Specific Protease 7<\/strong>
      Valles GJ, Jaiswal N, Korzhnev DM, Bezsonova I.
      bioRxiv. 2023 Jan 12:2023.01.11.523550.
      doi: 10.1101\/2023.01.11.523550
      PMID: 36711877 (preprint)<\/p>\n

      Evolution of Rev7 interactions in eukaryotic TLS DNA polymerase Pol\u03b6<\/strong>
      McPherson KS, Rizzo AA, Erlandsen H, Chatterjee N, Walker GC, Korzhnev DM.
      J Biol Chem. 2023;299(2):102859.
      doi: 10.1016\/j.jbc.2022.102859
      PMID: 36592930<\/p>\n

      \n

      2022<\/h2>\n

      DNA sequence specificity reveals HLTF HIRAN role in trinucleotide repeat recognition<\/strong>
      Dusek CO, Dash RC, McPherson KS, Calhoun JT, Bezsonova I, Korzhnev DM, Hadden MK.
      Biochemistry. 2022.
      doi: 10.1021\/acs.biochem.2c00027
      PMID: 35608245<\/p>\n

      NMR resonance assignments of USP7 catalytic domain<\/strong>
      Valles G, Pozhidaeva A, Korzhnev DM, Bezsonova I.
      Biomol NMR Assign. 2022;16(2):197\u2013203.
      doi: 10.1007\/s12104-022-10079-2
      PMID: 35536398<\/p>\n

      ILV methyl NMR assignments of E. coli \u03b2 clamp<\/strong>
      Lim S, Mahdi S, Beuning PJ, Korzhnev DM.
      Biomol NMR Assign. 2022;16(2):317\u2013323.
      doi: 10.1007\/s12104-022-10097-0
      PMID: 35687262<\/p>\n

      Architecture of two metal-binding sites in prolactin<\/strong>
      Vang J, Pustovalova Y, Korzhnev DM, Gorbatyuk O, Keeler C, Hodsdon ME, Hoch JC.
      Biophys J. 2022;121(7):1312\u20131321.
      doi: 10.1016\/j.bpj.2022.02.024
      PMID: 35192840<\/p>\n

      \n

      2021<\/h2>\n

      REV1 inhibition enhances radioresistance and autophagy<\/strong>
      Ikeh KE, Lamkin EN, Crompton A, Deutsch J, Fisher KJ, Gray M, Argyle DJ, Lim WY, Korzhnev DM, Hadden MK, Hong J, Zhou P, Chatterjee N.
      Cancers (Basel). 2021;13(21):5290.
      doi: 10.3390\/cancers13215290
      PMID: 34771454<\/p>\n

      Targeting protein-protein interactions in DNA damage response<\/strong>
      McPherson KS, Korzhnev DM.
      RSC Chem Biol. 2021;2(4):1167\u20131195.
      doi: 10.1039\/d1cb00101a
      PMID: 34458830<\/p>\n

      \n

      2019<\/h2>\n

      Rev1-Pol\u03b6 mutasome structure and inhibition<\/strong>
      Rizzo AA, Korzhnev DM.
      Enzymes. 2019;45:139\u2013181.
      doi: 10.1016\/bs.enz.2019.07.001
      PMID: 31627876<\/p>\n

      Virtual pharmacophore screening for Rev1 inhibitors<\/strong>
      Dash RC, Ozen Z, McCarthy KR, Chatterjee N, Harris CA, Rizzo AA, Walker GC, Korzhnev DM, Hadden MK.
      ChemMedChem. 2019;14(17):1610\u20131617.
      doi: 10.1002\/cmdc.201900307
      PMID: 31361935<\/p>\n

      Dynamics of \u03b2-clamp dimer interface<\/strong>
      Koleva BN, Gokcan H, Rizzo AA, Lim S, Jeanne Dit Fouque K, Choy A, Liriano ML, Fernandez-Lima F, Korzhnev DM, Cisneros GA, Beuning PJ.
      Biophys J. 2019;117(3):587\u2013601.
      doi: 10.1016\/j.bpj.2019.06.035
      PMID: 31349986<\/p>\n

      \n

      2018<\/h2>\n

      Rev7 dimerization in TLS complex assembly<\/strong>
      Rizzo AA, Vassel FM, Chatterjee N, D\u2019Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM.
      PNAS. 2018;115:E8191\u2013E8200.
      doi: 10.1073\/pnas.1801149115
      PMID: 30111544<\/p>\n

      Small molecules disrupting Rev1-CT\/RIR interaction<\/strong>
      Ozen Z, Dash RC, McCarthy KR, Chow SA, Rizzo AA, Korzhnev DM, Hadden MK.
      Bioorg Med Chem. 2018;26(14):4301\u20134309.
      doi: 10.1016\/j.bmc.2018.07.029
      PMID: 30037752<\/p>\n

      Structural scaffold identification for Rev1 targeting<\/strong>
      Dash RC, Ozen Z, Rizzo AA, Lim S, Korzhnev DM, Hadden MK.
      J Chem Inf Model. 2018;58(11):2266\u20132277.
      doi: 10.1021\/acs.jcim.8b00535
      PMID: 30289707<\/p>\n

      \n

      2017<\/h2>\n

      Protein folding by NMR<\/strong>
      Zhuravleva A, Korzhnev DM.
      Prog Nucl Magn Reson Spectrosc. 2017;100:52\u201377.
      doi: 10.1016\/j.pnmrs.2016.10.002
      PMID: 28552172<\/p>\n

      Small-molecule TLS inhibitors<\/strong>
      Sail V, Rizzo AA, Chatterjee N, Dash RC, Ozen Z, Walker GC, Korzhnev DM, Hadden MK.
      ACS Chem Biol. 2017;12(7):1903\u20131912.
      doi: 10.1021\/acschembio.6b01144
      PMID: 28541665<\/p>\n

      Early folding nucleation events<\/strong>
      Kukic P, Pustovalova Y, Camilloni C, Gianni S, Korzhnev DM, Vendruscolo M.
      J Am Chem Soc. 2017;139:6899\u20136910.
      doi: 10.1021\/jacs.7b01540
      PMID: 28401755<\/p>\n

      Clamp loader \u03b4-subunit assignments<\/strong>
      Alyami EM, Rizzo AA, Beuning PJ, Korzhnev DM.
      Biomol NMR Assign. 2017;11(2):169\u2013173.
      doi: 10.1007\/s12104-017-9741-z
      PMID: 28265855<\/p>\n

      \n

      2016<\/h2>\n

      Targeting translesion synthesis for cancer therapy<\/strong>
      Korzhnev DM, Hadden MK.
      J Med Chem. 2016;59(20):9321\u20139336.
      doi: 10.1021\/acs.jmedchem.6b00596
      PMID: 27362876<\/p>\n

      \n

      2015<\/h2>\n

      USP7\u2013ICP0 interaction structure<\/strong>
      Pozhidaeva AK, Mohni KN, Dhe-Paganon S, Arrowsmith CH, Weller SK, Korzhnev DM, Bezsonova I.
      J Biol Chem. 2015;290(38):22907\u201322918.
      doi: 10.1074\/jbc.M115.664805
      PMID: 26224631<\/p>\n

      HLTF HIRAN domain and fork reversal<\/strong>
      Kile AC, Chavez DA, Bacal J, Eldirany S, Korzhnev DM, Bezsonova I, Eichman BF, Cimprich KA.
      Mol Cell. 2015;58(6):1090\u20131100.
      doi: 10.1016\/j.molcel.2015.05.013
      PMID: 26051180<\/p>\n

      \n

      2014<\/h2>\n

      Rad18 zinc finger\u2013ubiquitin structure<\/strong>
      Rizzo AA, Salerno PE, Bezsonova I, Korzhnev DM.
      Biochemistry. 2014;53(37):5895\u20135906.
      doi: 10.1021\/bi500823h
      PMID: 25162118<\/p>\n

      \n

      2013<\/h2>\n

      Rev1\u2013PCNA interaction mapping<\/strong>
      Pustovalova Y, Maciejewski MW, Korzhnev DM.
      J Mol Biol. 2013;425(17):3091\u20133105.
      doi: 10.1016\/j.jmb.2013.05.029
      PMID: 23747975<\/p>\n

      Loss of structure\u2013gain of function (commentary)<\/strong>
      Korzhnev DM.
      J Mol Biol. 2013;425(1):17\u201318.
      doi: 10.1016\/j.jmb.2012.10.012
      PMID: 23084974<\/p>\n

      \n

      2012<\/h2>\n

      Rev1 C-terminal binding sites<\/strong>
      Pustovalova Y, Bezsonova I, Korzhnev DM.
      FEBS Lett. 2012;586(19):3051\u20133056.
      doi: 10.1016\/j.febslet.2012.07.021
      PMID: 22828282<\/p>\n

      NMR structure of Rev1\u2013Pol\u03b7 interaction<\/strong>
      Pozhidaeva A, Pustovalova Y, D\u2019Souza S, Bezsonova I, Walker GC, Korzhnev DM.
      Biochemistry. 2012;51(27):5506\u20135520.
      doi: 10.1021\/bi300566z
      PMID: 22691049<\/p>\n

      FF domain folding intermediate (PNAS)<\/strong>
      Korzhnev DM, Religa TL, Kay LE.
      PNAS. 2012;109(44):17777\u201317782.
      doi: 10.1073\/pnas.1201799109
      PMID: 22647611<\/p>\n

      Cross-validation of folding intermediate structure<\/strong>
      Barette J, Velyvis A, Religa TL, Korzhnev DM, Kay LE.
      J Phys Chem B. 2012;116(23):6637\u20136644.
      doi: 10.1021\/jp209974f
      PMID: 22148426<\/p>\n

      \n

      2011<\/h2>\n

      FF domain folding intermediate structure<\/strong>
      Korzhnev DM, Vernon RM, Religa TL, Hansen AL, Baker D, Fersht AR, Kay LE.
      J Am Chem Soc. 2011;133(28):10974\u201310982.
      doi: 10.1021\/ja203686t
      PMID: 21639149<\/p>\n

      \n

      2010<\/h2>\n

      Copper-binding domains NMR study<\/strong>
      Fatemi N, Korzhnev DM, Velyvis A, Sarkar B, Forman-Kay JD.
      Biochemistry. 2010;49(39):8468\u20138477.
      doi: 10.1021\/bi1008535
      PMID: 20799727<\/p>\n

      Chemical shift difference measurement method<\/strong>
      Bouvignies G, Korzhnev DM, Neudecker P, Hansen DF, Cordes MH, Kay LE.
      J Biomol NMR. 2010;47(2):135\u2013141.
      doi: 10.1007\/s10858-010-9418-8
      PMID: 20428928<\/p>\n

      R1\u03c1 vs HSQC comparison<\/strong>
      Auer R, Hansen DF, Neudecker P, Korzhnev DM, Muhandiram DR, Konrat R, Kay LE.
      J Biomol NMR. 2010;46(3):205\u2013216.
      doi: 10.1007\/s10858-009-9394-z
      PMID: 20033258<\/p>\n

      \n

      2009<\/h2>\n

      Ubiquitin\u2013SH3 interaction dynamics<\/strong>
      van Ingen H, Korzhnev DM, Kay LE.
      J Phys Chem B. 2009;113(29):9968\u20139977.
      doi: 10.1021\/jp902793y
      PMID: 19569643<\/p>\n

      \n

      2008<\/h2>\n

      Protein folding and relaxation dispersion review<\/strong>
      Korzhnev DM, Kay LE.
      Acc Chem Res. 2008;41(3):442\u2013451.
      doi: 10.1021\/ar700189y
      PMID: 18275162<\/p>\n

      \n

      2007<\/h2>\n

      MARK3 UBA instability<\/strong>
      Murphy JM, Korzhnev DM, Ceccarelli DF, Briant DJ, Zarrine-Afsar A, Sicheri F, Kay LE, Pawson T.
      PNAS. 2007;104(36):14336\u201314341.
      doi: 10.1073\/pnas.0703012104
      PMID: 17726107<\/p>\n

      FF domain folding pathway<\/strong>
      Korzhnev DM, Religa TL, Lundstr\u00f6m P, Fersht AR, Kay LE.
      J Mol Biol. 2007;372(2):497\u2013512.
      doi: 10.1016\/j.jmb.2007.06.012
      PMID: 17689561<\/p>\n

      Barnase dynamics propagation<\/strong>
      Zhuravleva A, Korzhnev DM, Nolde SB, Kay LE, Arseniev AS, Billeter M, Orekhov VY.
      J Mol Biol. 2007;367(4):1079\u20131092.
      doi: 10.1016\/j.jmb.2007.01.051
      PMID: 17306298<\/p>\n

      \n

      2006<\/h2>\n

      SH3 folding hydration and packing<\/strong>
      Bezsonova I, Korzhnev DM, Prosser RS, Forman-Kay JD, Kay LE.
      Biochemistry. 2006;45(15):4711\u20134719.
      doi: 10.1021\/bi060177r
      PMID: 16605239<\/p>\n

      Fyn SH3 folding intermediates<\/strong>
      Korzhnev DM, Neudecker P, Zarrine-Afsar A, Davidson AR, Kay LE.
      Biochemistry. 2006;45(34):10175\u201310183.
      doi: 10.1021\/bi0611560
      PMID: 16922492<\/p>\n

      SH3 relaxation dispersion analysis<\/strong>
      Neudecker P, Korzhnev DM, Kay LE.
      J Biomol NMR. 2006;34(3):129\u2013135.
      doi: 10.1007\/s10858-006-0001-2
      PMID: 16604422<\/p>\n

      \n

      2005<\/h2>\n

      SH3 folding side-chain interactions<\/strong>
      Mittermaier A, Korzhnev DM, Kay LE.
      Biochemistry. 2005;44(47):15430\u201315436.
      doi: 10.1021\/bi051771o
      PMID: 16300390<\/p>\n

      Enzyme intrinsic dynamics and catalysis<\/strong>
      Eisenmesser EZ, Millet O, Labeikovsky W, Korzhnev DM, Wolf-Watz M, Bosco DA, Skalicky JJ, Kay LE, Kern D.
      Nature. 2005;438(7064):117\u2013121.
      doi: 10.1038\/nature04105
      PMID: 16267559<\/p>\n

      Multiple-site exchange NMR dispersion<\/strong>
      Korzhnev DM, Neudecker P, Mittermaier A, Orekhov VY, Kay LE.
      J Am Chem Soc. 2005;127(44):15602\u201315611.
      doi: 10.1021\/ja054550e
      PMID: 16262426<\/p>\n

      Cross-correlated spin relaxation effects<\/strong>
      Korzhnev DM, Mittermaier AK, Kay LE.
      J Biomol NMR. 2005;31(4):337\u2013342.
      doi: 10.1007\/s10858-005-2468-7
      PMID: 15929000<\/p>\n

      Off-resonance R1\u03c1 dynamics<\/strong>
      Korzhnev DM, Orekhov VY, Kay LE.
      J Am Chem Soc. 2005;127(2):713\u2013721.
      doi: 10.1021\/ja0446855
      PMID: 15643897<\/p>\n

      \n

      2004<\/h2>\n

      Azurin electron transfer dynamics<\/strong>
      Zhuravleva AV, Korzhnev DM, Kupce E, Arseniev AS, Billeter M, Orekhov VY.
      J Mol Biol. 2004;342(5):1599\u20131611.
      doi: 10.1016\/j.jmb.2004.08.001
      PMID: 15364584<\/p>\n

      Fyn SH3 folding intermediates (Nature)<\/strong>
      Korzhnev DM, Salvatella X, Vendruscolo M, Di Nardo AA, Davidson AR, Dobson CM, Kay LE.
      Nature. 2004;430(6999):586\u2013590.
      doi: 10.1038\/nature02655
      PMID: 15282609<\/p>\n

      Multiple-quantum relaxation dispersion<\/strong>
      Korzhnev DM, Kloiber K, Kay LE.
      J Am Chem Soc. 2004;126(23):7320\u20137329.
      doi: 10.1021\/ja049968b
      PMID: 15186169<\/p>\n

      Protein L7\/L12 ribosome switching<\/strong>
      Bocharov EV, Sobol AG, Pavlov KV, Korzhnev DM, Jaravine VA, Gudkov AT, Arseniev AS.
      J Biol Chem. 2004;279(17):17697\u201317706.
      doi: 10.1074\/jbc.M313384200
      PMID: 14960595<\/p>\n

      Double- and zero-quantum NMR dispersion<\/strong>
      Orekhov VY, Korzhnev DM, Kay LE.
      J Am Chem Soc. 2004;126(6):1886\u20131891.
      doi: 10.1021\/ja038620y
      PMID: 14871121<\/p>\n

      Protein folding acceleration by nonnative stabilization<\/strong>
      Di Nardo AA, Korzhnev DM, Stogios PJ, Zarrine-Afsar A, Kay LE, Davidson AR.
      PNAS. 2004;101(21):7954\u20137959.
      doi: 10.1073\/pnas.0400550101
      PMID: 15148398<\/p>\n

      Methyl-TROSY for large proteins<\/strong>
      Korzhnev DM, Kloiber K, Kanelis V, Tugarinov V, Kay LE.
      J Am Chem Soc. 2004;126(12):3964\u20133973.
      doi: 10.1021\/ja039587i
      PMID: 15038751<\/p>\n

      \n

      2003<\/h2>\n

      T4 lysozyme exchange dynamics<\/strong>
      Korzhnev DM, Orekhov VY, Dahlquist FW, Kay LE.
      J Biomol NMR. 2003;26(1):39\u201348.
      doi: 10.1023\/a:1023039902737
      PMID: 12766401<\/p>\n

      Azurin low-populated states<\/strong>
      Korzhnev DM, Karlsson BG, Orekhov VY, Billeter M.
      Protein Sci. 2003;12(1):56\u201365.
      doi: 10.1110\/ps.0225403
      PMID: 12493828<\/p>\n

      \n

      2002<\/h2>\n

      TGF-\u03b23 dynamics-modulated activity<\/strong>
      Bocharov EV, Korzhnev DM, Blommers MJ, Arvinte T, Orekhov VY, Billeter M, Arseniev AS.
      J Biol Chem. 2002;277(48):46273\u201346279.
      doi: 10.1074\/jbc.M206274200
      PMID: 12221089<\/p>\n

      Heteronuclear spin-lock relaxation measurement<\/strong>
      Korzhnev DM, Skrynnikov NR, Millet O, Torchia DA, Kay LE.
      J Am Chem Soc. 2002;124(36):10743\u201310753.
      doi: 10.1021\/ja0204776
      PMID: 12207529<\/p>\n

      \n

      2001\u20131995<\/h2>\n

      Zervamicin backbone dynamics<\/strong>
      Korzhnev DM, Bocharov EV, Zhuravlyova AV, Orekhov VY, Ovchinnikova TV, Billeter M, Arseniev AS.
      FEBS Lett. 2001;495(1\u20132):52\u201355.
      doi: 10.1016\/s0014-5793(01)02363-8
      PMID: 11322946<\/p>\n

      Off-resonance CPMG effects<\/strong>
      Korzhnev DM, Tischenko EV, Arseniev AS.
      J Biomol NMR. 2000;17(3):231\u2013237.
      doi: 10.1023\/a:1008348827208
      PMID: 10959630<\/p>\n

      Nanosecond dynamics and diffusion<\/strong>
      Orekhov VY, Korzhnev DM, Pervushin KV, Hoffmann E, Arseniev AS.
      J Biomol Struct Dyn. 1999;17(1):157\u2013174.
      doi: 10.1080\/07391102.1999.10508348
      PMID: 10496429<\/p>\n

      Model-free dynamics limitations<\/strong>
      Korzhnev DM, Orekhov VY, Arseniev AS.
      J Magn Reson. 1997;127(2):184\u2013191.
      doi: 10.1006\/jmre.1997.1190
      PMID: 9281482<\/p>\n

      Bacterioopsin backbone dynamics<\/strong>
      Orekhov VY, Pervushin KV, Korzhnev DM, Arseniev AS.
      J Biomol NMR. 1995;6(2):113\u2013122.
      doi: 10.1007\/BF00211774
      PMID: 22910799<\/p>\n

      Helical subunit dynamics in bacterioopsin<\/strong>
      Pervushin KV, Orekhov VY, Korzhnev DM, Arseniev AS.
      J Biomol NMR. 1995;5(4):383\u2013396.
      doi: 10.1007\/BF00182282
      PMID: 22911558<\/p>\n<\/div>\n\t\t<\/div><\/div>

      <\/div><\/div><\/div>","protected":false},"excerpt":{"rendered":"

      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 […]<\/p>\n","protected":false},"author":304,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"_acf_changed":false,"footnotes":""},"acf":[],"publishpress_future_action":{"enabled":false,"date":"2026-06-14 11:37:50","action":"change-status","newStatus":"draft","terms":[],"taxonomy":""},"_links":{"self":[{"href":"https:\/\/health.uconn.edu\/bezsonova-lab\/wp-json\/wp\/v2\/pages\/266"}],"collection":[{"href":"https:\/\/health.uconn.edu\/bezsonova-lab\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/health.uconn.edu\/bezsonova-lab\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/health.uconn.edu\/bezsonova-lab\/wp-json\/wp\/v2\/users\/304"}],"replies":[{"embeddable":true,"href":"https:\/\/health.uconn.edu\/bezsonova-lab\/wp-json\/wp\/v2\/comments?post=266"}],"version-history":[{"count":28,"href":"https:\/\/health.uconn.edu\/bezsonova-lab\/wp-json\/wp\/v2\/pages\/266\/revisions"}],"predecessor-version":[{"id":781,"href":"https:\/\/health.uconn.edu\/bezsonova-lab\/wp-json\/wp\/v2\/pages\/266\/revisions\/781"}],"wp:attachment":[{"href":"https:\/\/health.uconn.edu\/bezsonova-lab\/wp-json\/wp\/v2\/media?parent=266"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}