|Date of 1st Appointment: 11th of August 2005
Present Appointment: Associate Professor
● Academic Qualification
2002 Ph.D. (habil.) in Biochemistry and Molecular Biology, University of the Saarland, Germany
2001 Ph.D. (habil.) in Biochemistry, University of Osnabrück, Germany
1995 Ph.D. (rer. nat.) in Biochemistry, Johannes Gutenberg-University Mainz, Germany
1992 Diploma Degree, Johannes Gutenberg-University Mainz, Germany
1995 - 1996, Postdoc-Fellowship of the German academical exchange service (DAAD)
1997 - 1999, Fellowship of the Human Frontiers Science Programs (HFSP)
2000 - 2001, Habilitation-Fellow of the German Research Foundation (DFG)
● Administrative involvements
1. Deputy Head of Division of Structural and Computational Biology, School of Biological Sciences,
Nanyang Technological University
2. Member of the Steering committee of the Singapore Bioimaging Consortium (SBIC)
The research group on Structure and function of molecular motors of A/Prof. G. Gruber in the Division of Structural and Computational Biology, SBS, NTU, is recognized for their expertise in determining the relationships between the structure and function of the so-called A1AO ATP synthases, V1VO ATPases, F1FO ATP synthases and AAA-ATPases. These enzymes are proposed to be the smallest biological motor proteins (nano-motor proteins). In order to get inside into the structure of these multi-subunit membrane complexes techniques like single particle analysis of electron micrographs, solution X-ray scattering, X-ray crystallography and NMR-spectroscopy are used. The functional and dynamical processes inside these enzymes are studied by fluorescence spectroscopy (e.g. FRET, FCS, intrinsic fluorescence spectroscopy) and biochemical approaches.
- An Integrated Framework to Study the Dynamics of BiologicalStructures
- Biological nanomotors for drug delivery and energy production
- Defining the structural traits of subunits D and E of the biological energy producer A1A0 ATPsynthase
- Functional and mechanistic understanding of the biological motor protein F1F0 ? ATP synthase due to structural approaches
- Functional and structural characterization of functional domains of the Reticulocyte Binding Proteins of Plasmodium during merozoite invasion
- Insights into the mechanisms and structure of the key coupling subunits and of the Mycobacterium tuberculosis F1FO ATP synthase, and their potential as novel TB drug target
- RESEARCH PACKAGE(3 YEARS)
- START-UP GRANT
- Structrual and biochemical characterization of the nucleotide-binding subunits A and B and the A-H interaction inside the archaea type A1A0ATPsynthase
- Structural and mechanistic understanding of HAMLET, a tumouricidal protein
- Target Based discovery of next generation pyrazinamide
- Targeting Oxidative Phosphorylation for the Rational Development of Sterilising Drug Combination for Drug-resistant Tuberculosis
- Touch the Molecule
- Understanding the Transition State and Assembly Formation of the Escherichia coli Alkyl Hyperoxide Reductase complex, an Essential Enzyme to alleviate Oxidative Stress
- Understanding the mechanisms and structure of the Mycobacterium tuberculosis bifunctional (p)ppGpp synthase/hydrolase, RelMtb
- Understanding the structure and assembly of subunits E,F,G and a of nature's most versatile pump, V-ATPase
- Understanding the structure and mechanisms of the Alkylhydroperoxide Reductase subunits C and F, a key enzyme ensemble for Antioxidant defence in vancomycin-resistant Enterococcus faecalis
- Bogdanović N, Sundararaman L, Kamariah N, Tyagi A, Bhushan S, Ragunathan P, Shin J, Dick T, Grüber G. (2018). Structure and function of Mycobacterium-specific components of F-ATP synthase subunits α and ε.. Journal of Structural Biology, 204(3), 420-434.
- Joon S1, Ragunathan P, Sundararaman L, Nartey W, Kundu S, Manimekalai MSS, Bogdanović N, Dick T, Grüber G. (2018). The NMR solution structure of Mycobacterium tuberculosis F-ATP synthase subunit ε provides new insight into energy coupling inside the rotary engine.. The FEBS Journal, 6(285), 1111-1128.
- Hao C, Gabryelczyk B, Manimekalai MSS, Gruber G, Salentinig S, Miserez A. (2017). Self-Coacervation of Modular Squid Beak Proteins – A Comparative Study. Soft Matter, 13(42), 7740-7752.
- Gopal P, Nartey W, Ragunathan P, Sarathy JP, Kaya F, Yee M, Setzer C, Manimekalai MSS, Dartois V, Grüber G, Dick T. (2017). Pyrazinoic acid inhibits mycobacterial coenzyme A biosynthesis by binding to aspartate decarboxylase PanD. ACS Infectious Diseases, 3(11), 807-819.
- Toh YK, Balakrishna AM, Manimekalai MSS, Chionh BB, Seetharaman RRC, Eisenhaber F, Eisenhaber B, Gruber G. (2017). Novel insights into the vancomycin-resistant Enterococcus faecalis (V583) alkylhydroperoxide reductase subunit F. Biochimica et biophysica acta - General Subjects, .