Advanced Studies of Membrane Proteins Lab

The lab team is focused on structural and biophysical studies of membrane proteins, such as ion channels, transporters, photoactive proteins, G protein-coupled receptors (GPCRs), transmembrane enzymes and their complexes.

The lab team is focused on structural and biophysical studies of membrane proteins, such as ion channels, transporters, photoactive proteins, G protein-coupled receptors (GPCRs), transmembrane enzymes and their complexes. Membrane proteins play a crucial role in many physiological processes mainly involved in signal transduction and membrane transport. Their dysfunction leads to many severe health disorders such as various types of cancer, chronic inflammations, cardiovascular diseases, neurodegenerative disorders. High resolution structures of these proteins are of great importance for understanding underlying mechanisms of these diseasesand to develop rational approaches to cure them. Despite the high importance there is still no structural information for a majority of membrane proteins existing, mainly because they are difficult to handle due to their amphiphilic nature and low stability. In our lab we established the infrastructure to purify and stabilize proteins from heterologous expression systems, such as E. coli, cell free and baculovirus expression systems. A variety of biophysical methods is available for structural and spectroscopic investigations of these protein systems. One of the core methods is the X-ray crystallography of membrane proteins. For this purpose we have setup a unique equipment for high throughput in meso crystallization, crystal imaging and crystallization process investigations. A Rigaku X-Ray HighFlux HomeLab is an important facility in use to characterize the quality of crystals and of proteins in solution. Advantages of modern fluorescence microscopy methods (including CLSM with Spectral Imaging, TIRFM, FCS, FCCS, 2PFM, FLIM, FRAP, SIM, PALM, direct STORM) realized in the Light Nanoscope facility is utilized for investigations of the dynamic properties of proteins and their behavior in a cellular environment. Protein targets can be further characterized with Brucker Ultraflextreme Mass Spectrometry, analytical HPLC system and differential fluorimetry to study protein thermostability.

Georg Bueldt

Director of the Advanced Studies of Membrane Proteins Laboratory

Education
1969 Diploma in Physics at the Technical University Berlin 

1972 Dissertation (Dr. rer. nat.) in Physical Chemistry, University of Mainz
Professional experience
1969 Diploma in Physics at the Technical University Berlin

1972 Dissertation (Dr. rer. nat.) in Physical Chemistry, University of Mainz

1978 Habilitation in Biophysics at the Biocenter of the University of Basel, Switzerland 

1982 - 1992 C2-Professor at the Physics Department of the Free University Berlin 

1993 - 2008 C4-Professor for Physical Biology at the Heinrich-Heine-University Düsseldorf, Germany 

1993 - 2011 Director at the Institute of Complex Systems (ICS) of the Research Center Jülich, ICS-5: Molecular Biophysics 

1996 Offer of a chair in Biophysics at the Johann-Wolfgang-Goethe University Frankfurt, which was rejected 

2004 - 2010 Speaker of the Virtual Institute for Structural Biology 

2011 - 2013 Founding Director of the Laboratory of Advanced Studies of Membrane Proteins at Moscow Institute of Physics and Technology (MIPT) 

Since 2014 Continuation as a Director of this Laboratory
Academic Interests
Systems: Membrane proteins and proteins of signal amplification cascades; mechanisms for the transport of protons and signals across membranes; protein folding. 

Methods: X-ray, neutron and electron diffraction on 2D and 3D protein crystals, crystal structures of intermediate states in the working cycle of proteins; micro-spectroscopy on single crystals trapped in intermediate states (visible, infrared); inelastic neutron scattering on equilibrium fluctuations in proteins, single molecule fluorescence spectroscopy.
Publications

2015, NATURE STRUCTURAL & MOLECULAR BIOLOGY (11.633)

2014, ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY (7.232)

2013, JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY (2.803)

2012, NEW JOURNAL OF PHYSICS (3.671)

2011, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (9.809)

2011, JOURNAL OF MOLECULAR BIOLOGY (3.959)

2010, ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY (7.232)

2008, JOURNAL OF SURFACE INVESTIGATION-X-RAY SYNCHROTRON AND NEUTRON TECHNIQUES (0.359)

Contacts
Phone +49 2461 61-2030
Email g.bueldt@fz-juelich.de

Valentin Borshchevskiy

Vice-Head of the Advanced Studies of Membrane Proteins Laboratory

Publications

2015, NATURE STRUCTURAL & MOLECULAR BIOLOGY (11.633)

2014, ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY (7.232)

2013, JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY (2.803)

2013, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (9.809)

2013, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (9.809)

2011, JOURNAL OF MOLECULAR BIOLOGY (3.959)

2010, ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY (7.232)

2008, JOURNAL OF SURFACE INVESTIGATION-X-RAY SYNCHROTRON AND NEUTRON TECHNIQUES (0.359)

FEBS JOURNAL (3.986)

Structure of the light-driven sodium pump KR2 and its implications for optogenetics

Gushchin I., Shevchenko V., Polovinkin V., Borshchevskiy V., Buslaev P., Bamberg E., Gordeliy V.

2002

NATURE (42.351)

Molecular basis of transmembrane signalling by sensory rhodopsin II-transducer complex

Gordeliy, VI, Labahn, J, Moukhametzianov, R, Efremov, R, Granzin, J, Schlesinger, R, Buldt, G, Savopol, T, Scheidig, AJ, Klare, JP, Engelhard, M

2004

BIOPHYSICAL JOURNAL (3.832)

2005

FEBS LETTERS (3.341)

Functional characterization of sensory rhodopsin II from Halobacterium salinarum expressed in Escherichia coli

Mironova, OS, Efremova, RG, Person, B, Heberle, J, Budyak, IL, Buldt, G, Schlesinger, R

JOURNAL OF CRYSTAL GROWTH (1.693)

Crystallization of F1F0-ATP synthase from Chloroflexus aurantiacus

Kiselyova, OI, Shiryaeva, GN, Efremov, RG, Gordeliy, VI, Yaminsky, IV, Yanyushin, MF, Buldt, G, Yaguzhinsky, LS

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES (3.096)

Particles of liquid-crystalline dispersions formed by (nucleic acid-rare earth element) complexes as a potential platform for neutron capture therapy

Yevdokimov, YM, Salyanov, VI, Kondrashina, OV, Borshevsky, VI, Semenov, SV, Gasanov, AA, Reshetov, IV, Kuznetsov, VD, Nikiforov, VN, Akulinichev, SV, Mordovskoi, MV, Potashev, SI, Skorkin, VM

2006

NATURE (42.351)

Development of the signal in sensory rhodopsin and its transfer to the cognate transducer

Moukhametzianov, R, Klare, JP, Efremov, R, Baeken, C, Goppner, A, Labahn, J, Engelhard, M, Buldt, G, Gordeliy VI

2008

JOURNAL OF SURFACE INVESTIGATION-X-RAY SYNCHROTRON AND NEUTRON TECHNIQUES (0.359)

Comparative analysis of sensory rhodopsin II structures in complex with a transducer and without it

Reshetnyak A.B., Borshchevskiy V.I., Klare J., Moiseeva E.S., Engelhardt M., Buldt G., Gordeliy V.I.

2009

JOURNAL OF SURFACE INVESTIGATION-X-RAY SYNCHROTRON AND NEUTRON TECHNIQUES (0.359)

2010

JOURNAL OF CRYSTAL GROWTH (1.693)

Isoprenoid-chained lipid beta-XylOC(16+4)-A novel molecule for in meso membrane protein crystallization

Borshchevskiy, V, Moiseeva, E, Kuklin, A, Buldt, G, Hato, M, Gordeliy, V

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY (7.232)

Overcoming merohedral twinning in crystals of bacteriorhodopsin grown in lipidic mesophase

Borshchevskiy, V, Efremov, R, Moiseeva, E, Buldt, G, Gordeliy, V

2011

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (9.809)

Conformational dynamics of helix 8 in the GPCR rhodopsin controls arrestin activation in the desensitization process

Kirchberg, K, Kim, TY, Moller, M, Skegro, D, Raju, GD, Granzin, J, Buldt, G, Schlesinger, R, Alexiev, U

JOURNAL OF MOLECULAR BIOLOGY (3.959)

Active State of Sensory Rhodopsin II: Structural Determinants for Signal Transfer and Proton Pumping

Gushchin, I, Reshetnyak, A, Borshchevskiy, V, Ishchenko, A, Round, E, Grudinin, S, Engelhard, M, Buldt, G, Gordeliy, V

JOURNAL OF MOLECULAR BIOLOGY (3.959)

X-ray-Radiation-Induced Changes in Bacteriorhodopsin Structure

Borshchevskiy, VI, Round, ES, Popov, AN, Buldt, G, Gordeliy, VI

2012

JOURNAL OF MOLECULAR BIOLOGY (3.959)

Crystal Structure of p44, a Constitutively Active Splice Variant of Visual Arrestin

Granzin, J, Cousin, A, Weirauch, M, Schlesinger, R, Buldt, G, Batra-Safferling, R

NEW JOURNAL OF PHYSICS (3.671)

Soft x-ray tomoholography

Guehrs, E, Stadler, AM, Flewett, S, Frommel, S, Geilhufe, J, Pfau, B, Rander, T, Schaffert, S, Buldt, G, Eisebitt, S

2013

JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY (2.803)

Ground state structure of D75N mutant of sensory rhodopsin II in complex with its cognate transducer

Ishchenko, A, Round, E, Borshchevskiy, V, Grudinin, S, Gushchin, I, Klare, JP, Balandin, T, Remeeva, A, Engelhard, M, Buldt, G, Gordeliy, V

NATURE (42.351)

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (9.809)

Structural insights into the proton pumping by unusual proteorhodopsin from nonmarine bacteria (vol 110, pg 12631, 2013)

Gushchin, I, Chervakov, P, Kuzmichev, P, Popov, AN, Round, E, Borshchevskiy, V, Ishchenko, A, Petrovskaya, L, Chupin, V, Dolgikh, DA, Arseniev, AS, Kirpichnikov, M, Gordeliy, V

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (9.809)

Structural insights into the proton pumping by unusual proteorhodopsin from nonmarine bacteria

Gushchin, I, Chervakov, P, Kuzmichev, P, Popov, AN, Round, E, Borshchevskiy, V, Ishchenko, A, Petrovskaya, L, Chupin, V, Dolgikh, DA, Arseniev, AA, Kirpichnikov, M, Gordeliy, V

2014

PLOS ONE (3.534)

Crystal Structure of Escherichia coli-Expressed Haloarcula marismortui Bacteriorhodopsin I in the Trimeric Form

Shevchenko, V, Gushchin, I, Polovinkin, V, Round, E, Borshchevskiy, V, Utrobin, P, Popov, A, Balandin, T, Buldt, G, Gordeliy, V

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY (7.232)

Low-dose X-ray radiation induces structural alterations in proteins

Borshchevskiy, V, Round, E, Erofeev, I, Weik, M, Ishchenko, A, Gushchin, I, Mishin, A, Willbold, D, Buldt, G, Gordeliy, V

CHEMBIOCHEM (3.06)

JOURNAL OF MEMBRANE BIOLOGY (2.174)

Nanoparticle Surface-Enhanced Raman Scattering of Bacteriorhodopsin Stabilized by Amphipol A8-35

Polovinkin, V, Balandin, T, Volkov, O, Round, E, Borshchevskiy, V, Utrobin, P, von Stetten, D, Royant, A, Willbold, D, Arzumanyan, G, Chupin, V, Popot, JL, Gordeliy, V

JOURNAL OF MEMBRANE BIOLOGY (2.174)

High-Resolution Structure of a Membrane Protein Transferred from Amphipol to a Lipidic Mesophase

Polovinkin, V, Gushchin, I, Sintsov, M, Round, E, Balandin, T, Chervakov, P, Schevchenko, V, Utrobin, P, Popov, A, Borshchevskiy, V, Mishin, A, Kuklin, A, Willbold, D, Chupin, V, Popot, JL, Gordeliy, V

NATURE COMMUNICATIONS (10.742)

X-ray structure of a CDP-alcohol phosphatidyltransferase membrane enzyme and insights into its catalytic mechanism

Nogly, P, Gushchin, I, Remeeva, A, Esteves, AM, Borges, N, Ma, P, Ishchenko, A, Grudinin, S, Round, E, Moraes, I, Borshchevskiy, V, Santos, H, Gordeliy, V, Archer, M

2015

NATURE STRUCTURAL & MOLECULAR BIOLOGY (11.633)

Crystal structure of a light-driven sodium pump

Gushchin, I, Shevchenko, V, Polovinkin, V, Kovalev, K, Alekseev, A, Round, E, Borshchevskiy, V, Balandin, T, Popov, A, Gensch, T, Fahlke, C, Bamann, C, Willbold, D, Buldt, G, Bamberg, E, Gordeliy, V

CRYSTAL GROWTH & DESIGN (4.558)

Nucleation and Growth of Membrane Protein Crystals in Meso - A Fluorescence Microscopy Study

Bogorodskiy A., Frolov F., Mishin A., Round E., Polovinkin V., Cherezov V., Gordeliy V., Büldt G., Gensch T., Borshchevskiy V.

PLOS ONE (3.534)

An Approach to Heterologous Expression of Membrane Proteins. The Case of Bacteriorhodopsin

Bratanov, D, Balandin, T, Round, E, Shevchenko, V, Gushchin, I, Polovinkin, V, Borshchevskiy, V, Gordeliy, V

PLOS ONE (3.534)

Structural and Functional Investigation of Flavin Binding Center of the NqrC Subunit of Sodium-Translocating NADH: Quinone Oxidoreductase from Vibrio harveyi

Borshchevskiy, V, Round, E, Bertsova, Y, Polovinkin, V, Gushchin, I, Ishchenko, A, Kovalev, K, Mishin, A, Kachalova, G, Popov, A, Bogachev, A, Gordeliy, V

Institut de Biologie Structurale Jean-Pierre Ebel (IBS)

European Synchrotron Radiation Facility (ESRF)

European Molecular Biology Laboratory (EMBL)