Dr. KATALIN E. KÖVÉR

full professor

 

 

University of Debrecen

Faculty of Science and Technology
Department of Inorganic and Analytical Chemistry
Debrecen, Hungary

 

flagA magyar változathoz kattintson a zászlóra.                                         

 


Office address:       University of Debrecen, Department of Inorganic and Analytical Chemistry
                                               H-4002 Debrecen P.O. Box 400, Hungary
                                               telephone: + 36 52 512900 ext.: 22370
                                               fax: + 36 52 489667
                                               e-mail: kover@science.unideb.hu



Academic degrees:

1979

M.Sc. in chemistry, Lajos Kossuth University, Debrecen, Hungary

1984

Ph.D. Lajos Kossuth University, Debrecen, Hungary

1988

C.Sc. (Candidate of Sciences), Hungarian Academy of Sciences

2002

D.Sc. (Doctor of Sciences), Hungarian Academy of Sciences

2013  

Member of the Hungarian Academy of Sciences

 

 

Professional career:

1979-84   

Research Fellow - BIOGAL Pharmaceutical Works - Department of Organic Chemistry,

L. Kossuth University, Debrecen

 

1984-88   

Research Associate - BIOGAL Pharmaceutical Works - Department of Organic Chemistry,

L. Kossuth University, Debrecen

 

1988-96   

Senior Research Associate - BIOGAL Pharmaceutical Works - Department of Organic Chemistry, 

L. Kossuth University, Debrecen

 

1996-99   

Senior Research Associate - Department of  Organic Chemistry,

L. Kossuth University, Debrecen

 

1999-2003   

Senior Research Associate - Department of Inorganic and Analytical Chemistry, University of Debrecen

 

2003-2008  

Distinguished Researcher - Department of Inorganic and Analytical Chemistry, University of Debrecen

 

2008-  

Full Professor - Department of Inorganic and Analytical Chemistry, University of Debrecen

 

Professional trips:

1987  

University of Illinois, Department of Biochemistry, Chicago, USA

1991-1993 

Department of Chemistry, The University of Arizona, USA

1995

Department of Chemistry, University of Arizona, Tucson, USA

1997

Department of Chemistry, University of Arizona, Tucson, USA

1998

Departamento de Espectroscopia y Estructura Molecular. Instituto de Quimica Fisica "Rocasolano". CSIC, Madrid, Spain

1999

Department of Inorganic, Physical and Structural Chemistry

visiting professor, Stockholm University, Sweden

1999

Department of Chemistry, University of Arizona, Tucson, USA

2002

MTA-OTKA-NSF, Department of Chemistry, University of Arizona, Tucson, USA

2003

Stockholm University, Department of Physico-Chemistry, Sweden

2004, 2005

University of Cape Town, Department of Computation Chemistry, Cape Town, South Africa

2005

CSIC, Madrid, Spain

2006

Department of Chemistry, University of Arizona, Tucson, USA

 

Awards:

 

Erdey L. Award from the Hungarian Academy of Sciences for NMR methodological developments, 1986
Széchenyi fellow from the Ministry of Education, Hungary, 1998-2001
 


Membership of Professional Societies:

·         Working Committee of NMR Spectroscopy (Hungarian Academy of Sciences)

·         Working Committee of Molecular Spectroscopy (Hungarian Academy of Sciences)

·         Working Committee of Research for Antibiotics (Hungarian Academy of Sciences)

 

          

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Research interest

 

 

 

 

 

 


Current research topics

 

    NMR methodological developments for sensitive and accurate measurement of homo- and heteronuclear coupling constants, relaxation rates and relaxation interference effects. Residual dipolar coupling constant (RDC). Pure shift (PS) experiments.

    NMR of biologically active oligopeptides, proteins, carbohydrates and natural products.

    NMR structure and dynamics of proteins. Molecular recognition and interactions. Application of TROSY-approach.

    Ligand-protein interactions studied by NMR and molecular modelling.

 

Number of publications: 201         

          

·         List of publications: MTMT, ResearchGate

 

Number of independent citations: 2553

 

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Ongoing projects

 


A novel two-dimensional method, SEA XLOC, for distinguishing two- and three-bond correlations in heteronuclear NMR-spectroscopy is introduced and
demonstrated on ibuprofen and by the complete set of correlations to a simple and a most complex quaternary 13C multiplet in strychnine.

Gyöngyösi T, Nagy TM, Kövér KE, Sørensen Ole W

Distinguishing between two- and three-bond correlations for all
13C multiplicities in heteronuclear NMR spectroscopy.

CHEMICAL COMMUNICATIONS 54:(70) pp. 9781-9784. (2018)

 

Imposing heteronuclear multiple-quantum multiplets on a 13C single-quantum spectrum distinguishes two- and three-bond correlations in an HMBC-type NMR spectrum.

http://dx.doi.org/10.1039/C8CC05156A

Researchgate project

 

 


The recently introduced CLIP-COSY (Koos et. al., 2016) experiment providing homonuclear correlation spectrum with high quality clean in-phase multiplets expedites the assignment of scalar coupled proton spin network and so, the structure elucidation of small and medium-sized molecules.
 

Gyöngyösi T, Timári I, Haller J, Koos M RM, Luy B, Kövér KE

Boosting the NMR assignment of carbohydrates with clean in-phase correlation experiments

CHEMPLUSCHEM 83:(1) pp. 53-60. (2018)

 

https://doi.org/10.1002/cplu.201700452

 

Left: Overlay of 1H–1H CLIP‐COSY and CLIP‐COSY
relayed (n=2) spectra of trisaccharide 1
Right: Representative 1D F2 traces demonstrate the high quality of spectra and the favorable
pure in‐phase character of the peaks.

 

 

 

 


The fundamental importance of protein-glycan recognition calls for specific and sensitive high-resolution techniques for their detailed analysis. After introduction of 19F NMR to study the recog­nition of fluorinated glycans, we present new 77Se NMR metho­dology for complementary studies of selenoglycans with optimised resolu­tion and sensitivity, where direct NMR detection on 77Se is replaced by its indirect observation in a 2D 1H, 77Se HSQMBC spectrum.
 

   

 


    The MEF2 transcription factors play crucial roles in muscle cell myogenesis and morphogenesis (Black et.al., 1998) Bioinformatical analysis indicates that the alternatively spliced β-domain of MEF2D does not fold into a well-defined structure and also remains to be conformationally heterogeneous in its bound state. To study the role of protein dynamics in the biological function, a series of 15-37 AA variants containing the MEF2D β-domain were designed. These peptide constructs differ in their predicted degree of fuzziness, i.e. dynamics in their bound state.
    Detailed analysis of the dynamical and structural properties of the peptides will give insights into the altered interaction patterns of the MEF2D β-domain corresponding to altered biological activities.

For the semi-automated assignment of these small and medium sized peptides novel NMR-experiments are being designed and utilized. The dynamics of the free peptides are studied using 15N relaxation measurements (T1, T2, heteronuclear NOE), from which spectral density functions are calculated. Random Coil Indexes (RCI) are determined from the chemical shifts (CA, CB, CO, N, HA) to derive model-free order parameters. Molecular dynamics simulations (MD) are also carried out to refine and validate the experimental results. Residue fluctuations, order parameters of the backbone amide bond vectors and the propensity of secondary structure elements are determined from the MD trajectories.



 

 

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Recent selected publications:

 

 

Gyöngyösi T, Nagy TM, Kövér KE, Sørensen Ole W

Distinguishing between two- and three-bond correlations for all 13C multiplicities in heteronuclear NMR spectroscopy.

CHEMICAL COMMUNICATIONS 54:(70) pp. 9781-9784. (2018)

 

Gyöngyösi T, Timári I, Haller J, Koos M RM, Luy B, Kövér KE

Boosting the NMR assignment of carbohydrates with clean in-phase correlation experiments

CHEMPLUSCHEM 83:(1) pp. 53-60. (2018)

 

Kónya Z, Bécsi B, Kiss A, Tamás I, Lontay B, Szilágyi L, Kövér KE, Erdődi F

Aralkyl selenoglycosides and related selenosugars in acetylated form activate protein phosphatase-1 and -2A

BIOORGANIC & MEDICINAL CHEMISTRY 26:(8) pp. 1875-1884. (2018)

 

Nagy TM, Knapp K, Illyés E, Timári I, Schlosser G, Csík G, Borics A, Majer Zs, Kövér KE

Photochemical and Structural Studies on Cyclic Peptide Models

MOLECULES 23:(9) Paper 2196. 20 p. (2018)

 

Timári I, Kövér KE

Broadband homonuclear decoupled HSQMBC methods.

MAGNETIC RESONANCE IN CHEMISTRY in press: Paper 14 December 2017. (2018)

 

Franco J, Sardi F, Szilágyi L, Kövér KE, Fehér K, Comini MA

Diglycosyl diselenides alter redox homeostasis and glucose consumption of infective African trypanosomes

INTERNATIONAL JOURNAL FOR PARASITOLOGY-DRUGS AND DRUG RESISTANCE 7:(3) pp. 303-313. (2017)

 

Fehér K, Timári I, Rákosi K, Szolomajer J, Illyés Tünde Z, Bartok A, Varga Z, Panyi G, Tóth G, Kövér KE

Probing pattern and dynamics of disulfide bridges using synthesis and NMR of an ion channel blocker peptide toxin with multiple diselenide bonds.

CHEMICAL SCIENCE 7:(4) pp. 2666-2673. (2016)

 

Hetényi A, Hegedüs Z, Fajka-Boja R, Monostori É, Kövér EK, Martinek TA

Target-specific NMR detection of protein–ligand interactions with antibody-relayed 15N-group selective STD

JOURNAL OF BIOMOLECULAR NMR 66:(4) pp. 227-232. (2016)

 

Timári I, Kaltschnee L, Raics MH, Roth F, Bell NGA, Adams RW, Nilsson M, Uhrin D, Morris GA, Thiele CM, Kövér KE

Real-time broadband proton-homodecoupled CLIP/CLAP-HSQC for automated measurement of heteronuclear one-bond coupling constants.

RSC ADVANCES 6:(91) pp. 87848-87855. (2016)

 

 

Timári I, Illyés TZ, Adams RW, Nilsson M, Szilágyi L, Morris GA, Kövér KE

Precise Measurement of Long-Range Heteronuclear Coupling Constants by a Novel Broadband Proton-Proton-Decoupled CPMG-HSQMBC Method.

CHEMISTRY-A EUROPEAN JOURNAL 21:(8) pp. 3472-3479. (2015)

 

 

Timári I, Szilágyi L, Kövér KE

PSYCHE CPMG-HSQMBC: An NMR Spectroscopic Method for Precise and Simple Measurement of Long-Range Heteronuclear Coupling Constants

CHEMISTRY-A EUROPEAN JOURNAL 21:(40) pp. 13939-13942. (2015)

 

Kaltschnee L, Kolmer A, Timári I, Schmidts V, Adams RW, Nilsson M, Kövér KE, Morris GA, Thiele CM

“Perfecting” pure shift HSQC: full homodecoupling for accurate and precise determination of heteronuclear couplings

CHEMICAL COMMUNICATIONS 50:(99) pp. 15702-15705. (2014)

 

Timári I, Kaltschnee L, Kolmer A, Adams RW, Nilsson M, Thiele CM, Morris GA, Kövér KE

Accurate determination of one-bond heteronuclear coupling constants with "pure shift" broadband proton-decoupled CLIP/CLAP-HSQC experiments

JOURNAL OF MAGNETIC RESONANCE 239: pp. 130-138. (2014)

 

 

 


 

Last update: March 1, 2019

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