{"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":"2024-03-20T09:58:47","modified_gmt":"2024-03-20T13:58:47","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

      1: Zhuravleva A, Korzhnev DM. Protein folding by NMR. Prog Nucl Magn Reson
      \nSpectrosc. 2017 May;100:52-77. doi: 10.1016\/j.pnmrs.2016.10.002. Epub 2016 Nov 9.
      \nReview. PubMed PMID: 28552172.<\/p>\n

      2: Sail V, Rizzo AA, Chatterjee N, Dash RC, Ozen Z, Walker GC, Korzhnev DM,
      \nHadden MK. Identification of Small Molecule Translesion Synthesis Inhibitors That
      \nTarget the Rev1-CT\/RIR Protein-Protein Interaction. ACS Chem Biol. 2017 Jul
      \n21;12(7):1903-1912. doi: 10.1021\/acschembio.6b01144. Epub 2017 Jun 9. PubMed
      \nPMID: 28541665.<\/p>\n

      3: Kukic P, Pustovalova Y, Camilloni C, Gianni S, Korzhnev DM, Vendruscolo M.
      \nStructural Characterization of the Early Events in the Nucleation-Condensation
      \nMechanism in a Protein Folding Process. J Am Chem Soc. 2017 May
      \n24;139(20):6899-6910. doi: 10.1021\/jacs.7b01540. Epub 2017 May 10. PubMed PMID:
      \n28401755.<\/p>\n

      4: Alyami EM, Rizzo AA, Beuning PJ, Korzhnev DM. NMR resonance assignments for
      \nthe N-terminal domain of the \u03b4 subunit of the E. coli \u03b3 clamp loader complex.
      \nBiomol NMR Assign. 2017 Mar 6. doi: 10.1007\/s12104-017-9741-z. [Epub ahead of
      \nprint] PubMed PMID: 28265855.<\/p>\n

      5: Korzhnev DM, Neculai D, Dhe-Paganon S, Arrowsmith CH, Bezsonova I. Solution
      \nNMR structure of the HLTF HIRAN domain: a conserved module in SWI2\/SNF2 DNA
      \ndamage tolerance proteins. J Biomol NMR. 2016 Nov;66(3):209-219. Epub 2016 Oct
      \n22. PubMed PMID: 27771863.<\/p>\n

      6: Korzhnev DM, Hadden MK. Targeting the Translesion Synthesis Pathway for the
      \nDevelopment of Anti-Cancer Chemotherapeutics. J Med Chem. 2016 Oct
      \n27;59(20):9321-9336. Epub 2016 Jul 19. Review. PubMed PMID: 27362876.<\/p>\n

      7: Pustovalova Y, Magalh\u00e3es MT, D'Souza S, Rizzo AA, Korza G, Walker GC, Korzhnev
      \nDM. Interaction between the Rev1 C-Terminal Domain and the PolD3 Subunit of Pol\u03b6
      \nSuggests a Mechanism of Polymerase Exchange upon Rev1\/Pol\u03b6-Dependent Translesion
      \nSynthesis. Biochemistry. 2016 Apr 5;55(13):2043-53. doi:
      \n10.1021\/acs.biochem.5b01282. Epub 2016 Mar 24. PubMed PMID: 26982350; PubMed
      \nCentral PMCID: PMC4898654.<\/p>\n

      8: Pozhidaeva AK, Mohni KN, Dhe-Paganon S, Arrowsmith CH, Weller SK, Korzhnev DM,
      \nBezsonova I. Structural Characterization of Interaction between Human
      \nUbiquitin-specific Protease 7 and Immediate-Early Protein ICP0 of Herpes Simplex
      \nVirus-1. J Biol Chem. 2015 Sep 18;290(38):22907-18. doi: 10.1074\/jbc.M115.664805.
      \nEpub 2015 Jul 29. PubMed PMID: 26224631; PubMed Central PMCID: PMC4645603.<\/p>\n

      9: Pustovalova Y, Kukic P, Vendruscolo M, Korzhnev DM. Probing the Residual
      \nStructure of the Low Populated Denatured State of ADA2h under Folding Conditions
      \nby Relaxation Dispersion Nuclear Magnetic Resonance Spectroscopy. Biochemistry.
      \n2015 Aug 4;54(30):4611-22. doi: 10.1021\/acs.biochem.5b00345. Epub 2015 Jul 21.
      \nPubMed PMID: 26115097.<\/p>\n

      10: Kile AC, Chavez DA, Bacal J, Eldirany S, Korzhnev DM, Bezsonova I, Eichman
      \nBF, Cimprich KA. HLTF's Ancient HIRAN Domain Binds 3' DNA Ends to Drive
      \nReplication Fork Reversal. Mol Cell. 2015 Jun 18;58(6):1090-100. doi:
      \n10.1016\/j.molcel.2015.05.013. Epub 2015 Jun 4. PubMed PMID: 26051180; PubMed
      \nCentral PMCID: PMC4475461.<\/p>\n

      11: Rizzo AA, Salerno PE, Bezsonova I, Korzhnev DM. NMR structure of the human
      \nRad18 zinc finger in complex with ubiquitin defines a class of UBZ domains in
      \nproteins linked to the DNA damage response. Biochemistry. 2014 Sep
      \n23;53(37):5895-906. doi: 10.1021\/bi500823h. Epub 2014 Sep 15. PubMed PMID:
      \n25162118.<\/p>\n

      12: Machado LE, Pustovalova Y, Kile AC, Pozhidaeva A, Cimprich KA, Almeida FC,
      \nBezsonova I, Korzhnev DM. PHD domain from human SHPRH. J Biomol NMR. 2013
      \nAug;56(4):393-9. doi: 10.1007\/s10858-013-9758-2. Epub 2013 Aug 2. PubMed PMID:
      \n23907177; PubMed Central PMCID: PMC3905319.<\/p>\n

      13: Pustovalova Y, Maciejewski MW, Korzhnev DM. NMR mapping of PCNA interaction
      \nwith translesion synthesis DNA polymerase Rev1 mediated by Rev1-BRCT domain. J
      \nMol Biol. 2013 Sep 9;425(17):3091-105. doi: 10.1016\/j.jmb.2013.05.029. Epub 2013
      \nJun 7. PubMed PMID: 23747975.<\/p>\n

      14: Korzhnev DM. Loss of structure-gain of function. J Mol Biol. 2013 Jan
      \n9;425(1):17-8. doi: 10.1016\/j.jmb.2012.10.012. Epub 2012 Oct 22. PubMed PMID:
      \n23084974.<\/p>\n

      15: Markley JL, Akutsu H, Asakura T, Baldus M, Boelens R, Bonvin A, Kaptein R,
      \nBax A, Bezsonova I, Gryk MR, Hoch JC, Korzhnev DM, Maciejewski MW, Case D, Chazin
      \nWJ, Cross TA, Dames S, Kessler H, Lange O, Madl T, Reif B, Sattler M, Eliezer D,
      \nFersht A, Forman-Kay J, Kay LE, Fraser J, Gross J, Kortemme T, Sali A, Fujiwara
      \nT, Gardner K, Luo X, Rizo-Rey J, Rosen M, Gil RR, Ho C, Rule G, Gronenborn AM,
      \nIshima R, Klein-Seetharaman J, Tang P, van der Wel P, Xu Y, Grzesiek S, Hiller S,
      \nSeelig J, Laue ED, Mott H, Nietlispach D, Barsukov I, Lian LY, Middleton D,
      \nBlumenschein T, Moore G, Campbell I, Schnell J, Vakonakis IJ, Watts A, Conte MR,
      \nMason J, Pfuhl M, Sanderson MR, Craven J, Williamson M, Dominguez C, Roberts G,
      \nG\u00fcnther U, Overduin M, Werner J, Williamson P, Blindauer C, Crump M, Driscoll P,
      \nFrenkiel T, Golovanov A, Matthews S, Parkinson J, Uhrin D, Williams M, Neuhaus D,
      \nOschkinat H, Ramos A, Shaw DE, Steinbeck C, Vendruscolo M, Vuister GW, Walters
      \nKJ, Weinstein H, W\u00fcthrich K, Yokoyama S. In support of the BMRB. Nat Struct Mol
      \nBiol. 2012 Sep;19(9):854-60. doi: 10.1038\/nsmb.2371. PubMed PMID: 22955930.<\/p>\n

      16: Pustovalova Y, Bezsonova I, Korzhnev DM. The C-terminal domain of human Rev1
      \ncontains independent binding sites for DNA polymerase \u03b7 and Rev7 subunit of
      \npolymerase \u03b6. FEBS Lett. 2012 Sep 21;586(19):3051-6. doi:
      \n10.1016\/j.febslet.2012.07.021. Epub 2012 Jul 22. PubMed PMID: 22828282; PubMed
      \nCentral PMCID: PMC3572780.<\/p>\n

      17: Pozhidaeva A, Pustovalova Y, D'Souza S, Bezsonova I, Walker GC, Korzhnev DM.
      \nNMR structure and dynamics of the C-terminal domain from human Rev1 and its
      \ncomplex with Rev1 interacting region of DNA polymerase \u03b7. Biochemistry. 2012 Jul
      \n10;51(27):5506-20. Epub 2012 Jun 28. PubMed PMID: 22691049; PubMed Central PMCID:
      \nPMC3732116.<\/p>\n

      18: Korzhnev DM, Religa TL, Kay LE. Transiently populated intermediate functions
      \nas a branching point of the FF domain folding pathway. Proc Natl Acad Sci U S A.
      \n2012 Oct 30;109(44):17777-82. doi: 10.1073\/pnas.1201799109. Epub 2012 May 30.
      \nPubMed PMID: 22647611; PubMed Central PMCID: PMC3497754.<\/p>\n

      19: Barette J, Velyvis A, Religa TL, Korzhnev DM, Kay LE. Cross-validation of the
      \nstructure of a transiently formed and low populated FF domain folding
      \nintermediate determined by relaxation dispersion NMR and CS-Rosetta. J Phys Chem
      \nB. 2012 Jun 14;116(23):6637-44. doi: 10.1021\/jp209974f. Epub 2011 Dec 23. PubMed
      \nPMID: 22148426.<\/p>\n

      20: Korzhnev DM, Vernon RM, Religa TL, Hansen AL, Baker D, Fersht AR, Kay LE.
      \nNonnative interactions in the FF domain folding pathway from an atomic resolution
      \nstructure of a sparsely populated intermediate: an NMR relaxation dispersion
      \nstudy. J Am Chem Soc. 2011 Jul 20;133(28):10974-82. doi: 10.1021\/ja203686t. Epub
      \n2011 Jun 28. PubMed PMID: 21639149; PubMed Central PMCID: PMC3705915.<\/p>\n

      21: Korzhnev DM, Religa TL, Banachewicz W, Fersht AR, Kay LE. A transient and
      \nlow-populated protein-folding intermediate at atomic resolution. Science. 2010
      \nSep 10;329(5997):1312-6. doi: 10.1126\/science.1191723. PubMed PMID: 20829478.<\/p>\n

      22: Fatemi N, Korzhnev DM, Velyvis A, Sarkar B, Forman-Kay JD. NMR
      \ncharacterization of copper-binding domains 4-6 of ATP7B . Biochemistry. 2010 Oct
      \n5;49(39):8468-77. doi: 10.1021\/bi1008535. Epub 2010 Sep 10. PubMed PMID:
      \n20799727.<\/p>\n

      23: Bouvignies G, Korzhnev DM, Neudecker P, Hansen DF, Cordes MH, Kay LE. A
      \nsimple method for measuring signs of (1)H (N) chemical shift differences between
      \nground and excited protein states. J Biomol NMR. 2010 Jun;47(2):135-41. doi:
      \n10.1007\/s10858-010-9418-8. Epub 2010 Apr 29. PubMed PMID: 20428928; PubMed
      \nCentral PMCID: PMC3034452.<\/p>\n

      24: Auer R, Hansen DF, Neudecker P, Korzhnev DM, Muhandiram DR, Konrat R, Kay LE.
      \nMeasurement of signs of chemical shift differences between ground and excited
      \nprotein states: a comparison between H(S\/M)QC and R1rho methods. J Biomol NMR.
      \n2010 Mar;46(3):205-16. doi: 10.1007\/s10858-009-9394-z. Epub 2009 Dec 22. PubMed
      \nPMID: 20033258.<\/p>\n

      25: van Ingen H, Korzhnev DM, Kay LE. An analysis of the effects of 1HN-(1)HN
      \ndipolar couplings on the measurement of amide bond vector orientations in
      \ninvisible protein states by relaxation dispersion NMR. J Phys Chem B. 2009 Jul
      \n23;113(29):9968-77. doi: 10.1021\/jp902793y. PubMed PMID: 19569643.<\/p>\n<\/div>\n\t\t<\/div><\/div>

      …<\/h3>\t\t\t

      26: Korzhnev DM, Bezsonova I, Lee S, Chalikian TV, Kay LE. Alternate binding
      \nmodes for a ubiquitin-SH3 domain interaction studied by NMR spectroscopy. J Mol
      \nBiol. 2009 Feb 20;386(2):391-405. doi: 10.1016\/j.jmb.2008.11.055. Epub 2008 Dec
      \n6. PubMed PMID: 19111555.<\/p>\n

      27: Korzhnev DM, Kay LE. Probing invisible, low-populated States of protein
      \nmolecules by relaxation dispersion NMR spectroscopy: an application to protein
      \nfolding. Acc Chem Res. 2008 Mar;41(3):442-51. doi: 10.1021\/ar700189y. Epub 2008
      \nFeb 15. Review. PubMed PMID: 18275162.<\/p>\n

      28: Murphy JM, Korzhnev DM, Ceccarelli DF, Briant DJ, Zarrine-Afsar A, Sicheri F,
      \nKay LE, Pawson T. Conformational instability of the MARK3 UBA domain compromises
      \nubiquitin recognition and promotes interaction with the adjacent kinase domain.
      \nProc Natl Acad Sci U S A. 2007 Sep 4;104(36):14336-41. Epub 2007 Aug 28. PubMed
      \nPMID: 17726107; PubMed Central PMCID: PMC1964837.<\/p>\n

      29: Korzhnev DM, Religa TL, Lundstr\u00f6m P, Fersht AR, Kay LE. The folding pathway
      \nof an FF domain: characterization of an on-pathway intermediate state under
      \nfolding conditions by (15)N, (13)C(alpha) and (13)C-methyl relaxation dispersion
      \nand (1)H\/(2)H-exchange NMR spectroscopy. J Mol Biol. 2007 Sep 14;372(2):497-512.
      \nEpub 2007 Jun 9. PubMed PMID: 17689561.<\/p>\n

      30: Zhuravleva A, Korzhnev DM, Nolde SB, Kay LE, Arseniev AS, Billeter M, Orekhov
      \nVY. Propagation of dynamic changes in barnase upon binding of barstar: an NMR and
      \ncomputational study. J Mol Biol. 2007 Apr 6;367(4):1079-92. Epub 2007 Jan 24.
      \nPubMed PMID: 17306298.
      \n31: Korzhnev DM, Neudecker P, Zarrine-Afsar A, Davidson AR, Kay LE. Abp1p and Fyn
      \nSH3 domains fold through similar low-populated intermediate states. Biochemistry.
      \n2006 Aug 29;45(34):10175-83. PubMed PMID: 16922492.<\/p>\n

      32: Korzhnev DM, Bezsonova I, Evanics F, Taulier N, Zhou Z, Bai Y, Chalikian TV,
      \nProsser RS, Kay LE. Probing the transition state ensemble of a protein folding
      \nreaction by pressure-dependent NMR relaxation dispersion. J Am Chem Soc. 2006 Apr
      \n19;128(15):5262-9. PubMed PMID: 16608362.<\/p>\n

      33: Bezsonova I, Korzhnev DM, Prosser RS, Forman-Kay JD, Kay LE. Hydration and
      \npacking along the folding pathway of SH3 domains by pressure-dependent NMR.
      \nBiochemistry. 2006 Apr 18;45(15):4711-9. PubMed PMID: 16605239.<\/p>\n

      34: Neudecker P, Korzhnev DM, Kay LE. Assessment of the effects of increased
      \nrelaxation dispersion data on the extraction of 3-site exchange parameters
      \ncharacterizing the unfolding of an SH3 domain. J Biomol NMR. 2006
      \nMar;34(3):129-35. PubMed PMID: 16604422.<\/p>\n

      35: Mittermaier A, Korzhnev DM, Kay LE. Side-chain interactions in the folding
      \npathway of a Fyn SH3 domain mutant studied by relaxation dispersion NMR
      \nspectroscopy. Biochemistry. 2005 Nov 29;44(47):15430-6. PubMed PMID: 16300390.<\/p>\n

      36: Eisenmesser EZ, Millet O, Labeikovsky W, Korzhnev DM, Wolf-Watz M, Bosco DA,
      \nSkalicky JJ, Kay LE, Kern D. Intrinsic dynamics of an enzyme underlies catalysis.
      \nNature. 2005 Nov 3;438(7064):117-21. PubMed PMID: 16267559.<\/p>\n

      37: Korzhnev DM, Neudecker P, Mittermaier A, Orekhov VY, Kay LE. Multiple-site
      \nexchange in proteins studied with a suite of six NMR relaxation dispersion
      \nexperiments: an application to the folding of a Fyn SH3 domain mutant. J Am Chem
      \nSoc. 2005 Nov 9;127(44):15602-11. PubMed PMID: 16262426.<\/p>\n

      38: Korzhnev DM, Mittermaier AK, Kay LE. Cross-correlated spin relaxation effects
      \nin methyl 1H CPMG-based relaxation dispersion experiments: complications and a
      \nsimple solution. J Biomol NMR. 2005 Apr;31(4):337-42. PubMed PMID: 15929000.<\/p>\n

      39: Korzhnev DM, Orekhov VY, Kay LE. Off-resonance R(1rho) NMR studies of
      \nexchange dynamics in proteins with low spin-lock fields: an application to a Fyn
      \nSH3 domain. J Am Chem Soc. 2005 Jan 19;127(2):713-21. PubMed PMID: 15643897.<\/p>\n

      40: Zhuravleva AV, Korzhnev DM, Kupce E, Arseniev AS, Billeter M, Orekhov VY.
      \nGated electron transfers and electron pathways in azurin: a NMR dynamic study at
      \nmultiple fields and temperatures. J Mol Biol. 2004 Oct 1;342(5):1599-611. PubMed
      \nPMID: 15364584.<\/p>\n

      41: Korzhnev DM, Salvatella X, Vendruscolo M, Di Nardo AA, Davidson AR, Dobson
      \nCM, Kay LE. Low-populated folding intermediates of Fyn SH3 characterized by
      \nrelaxation dispersion NMR. Nature. 2004 Jul 29;430(6999):586-90. PubMed PMID:
      \n15282609.<\/p>\n

      42: Korzhnev DM, Kloiber K, Kay LE. Multiple-quantum relaxation dispersion NMR
      \nspectroscopy probing millisecond time-scale dynamics in proteins: theory and
      \napplication. J Am Chem Soc. 2004 Jun 16;126(23):7320-9. PubMed PMID: 15186169.<\/p>\n

      43: Di Nardo AA, Korzhnev DM, Stogios PJ, Zarrine-Afsar A, Kay LE, Davidson AR.
      \nDramatic acceleration of protein folding by stabilization of a nonnative backbone
      \nconformation. Proc Natl Acad Sci U S A. 2004 May 25;101(21):7954-9. Epub 2004 May
      \n17. PubMed PMID: 15148398; PubMed Central PMCID: PMC419538.<\/p>\n

      44: Korzhnev DM, Kloiber K, Kanelis V, Tugarinov V, Kay LE. Probing slow dynamics
      \nin high molecular weight proteins by methyl-TROSY NMR spectroscopy: application
      \nto a 723-residue enzyme. J Am Chem Soc. 2004 Mar 31;126(12):3964-73. PubMed PMID:
      \n15038751.<\/p>\n

      45: Bocharov EV, Sobol AG, Pavlov KV, Korzhnev DM, Jaravine VA, Gudkov AT,
      \nArseniev AS. From structure and dynamics of protein L7\/L12 to molecular switching
      \nin ribosome. J Biol Chem. 2004 Apr 23;279(17):17697-706. Epub 2004 Feb 11. PubMed
      \nPMID: 14960595.<\/p>\n

      46: Orekhov VY, Korzhnev DM, Kay LE. Double- and zero-quantum NMR relaxation
      \ndispersion experiments sampling millisecond time scale dynamics in proteins. J Am
      \nChem Soc. 2004 Feb 18;126(6):1886-91. PubMed PMID: 14871121.<\/p>\n

      47: Korzhnev DM, Orekhov VY, Dahlquist FW, Kay LE. Off-resonance R1rho relaxation
      \noutside of the fast exchange limit: an experimental study of a cavity mutant of
      \nT4 lysozyme. J Biomol NMR. 2003 May;26(1):39-48. PubMed PMID: 12766401.<\/p>\n

      48: Korzhnev DM, Karlsson BG, Orekhov VY, Billeter M. NMR detection of multiple
      \ntransitions to low-populated states in azurin. Protein Sci. 2003 Jan;12(1):56-65.
      \nPubMed PMID: 12493828; PubMed Central PMCID: PMC2312403.<\/p>\n

      49: Bocharov EV, Korzhnev DM, Blommers MJ, Arvinte T, Orekhov VY, Billeter M,
      \nArseniev AS. Dynamics-modulated biological activity of transforming growth factor
      \nbeta3. J Biol Chem. 2002 Nov 29;277(48):46273-9. Epub 2002 Sep 6. PubMed PMID:
      \n12221089.<\/p>\n

      50: Korzhnev DM, Skrynnikov NR, Millet O, Torchia DA, Kay LE. An NMR experiment
      \nfor the accurate measurement of heteronuclear spin-lock relaxation rates. J Am
      \nChem Soc. 2002 Sep 11;124(36):10743-53. PubMed PMID: 12207529.<\/p>\n

      51: Korzhnev DM, Bocharov EV, Zhuravlyova AV, Orekhov VY, Ovchinnikova TV,
      \nBilleter M, Arseniev AS. Backbone dynamics of the channel-forming antibiotic
      \nzervamicin IIB studied by 15N NMR relaxation. FEBS Lett. 2001 Apr
      \n20;495(1-2):52-5. PubMed PMID: 11322946.<\/p>\n

      52: Korzhnev DM, Tischenko EV, Arseniev AS. Off-resonance effects in 15N T2 CPMG
      \nmeasurements. J Biomol NMR. 2000 Jul;17(3):231-7. PubMed PMID: 10959630.<\/p>\n

      53: Orekhov VY, Korzhnev DM, Pervushin KV, Hoffmann E, Arseniev AS. Sampling of
      \nprotein dynamics in nanosecond time scale by 15N NMR relaxation and
      \nself-diffusion measurements. J Biomol Struct Dyn. 1999 Aug;17(1):157-74. PubMed
      \nPMID: 10496429.<\/p>\n

      54: Korzhnev DM, Orekhov VY, Arseniev AS. Model-free approach beyond the borders
      \nof its applicability. J Magn Reson. 1997 Aug;127(2):184-91. PubMed PMID: 9281482.<\/p>\n

      55: Orekhov VY, Pervushin KV, Korzhnev DM, Arseniev AS. Backbone dynamics of
      \n(1-71)- and (1-36)bacterioopsin studied by two-dimensional (1)H- (15)N NMR
      \nspectroscopy. J Biomol NMR. 1995 Sep;6(2):113-22. doi: 10.1007\/BF00211774. PubMed
      \nPMID: 22910799.<\/p>\n

      56: Pervushin KV, Orekhov VY, Korzhnev DM, Arseniev AS. Manifestation of
      \nintramolecular motions on pico- and nanosecond time scales in (1)H- (15)N NMR
      \nrelaxation: Analysis of dynamic models of one- and two-helical subunits of
      \nbacterioopsin. J Biomol NMR. 1995 Jun;5(4):383-96. doi: 10.1007\/BF00182282.
      \nPubMed PMID: 22911558.<\/p>\n<\/div>\n\t\t<\/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":"2026-04-11 20:22:03","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":22,"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}]}}