|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.
- 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
- 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
- Touch the Molecule
- Understanding the structure and assembly of subunits E,F,G and a of nature's most versatile pump, V-ATPase
- Wei L, Jiang P, Manimekalai MSS, Hunke C, Gruber G, Pervushin K, Mu Y. (2013). Extended structure of rat islet amyloid polypeptide in solution. Advances in Experimental Medicine and Biology, .
- Basak s, Lim J, Manimekalai MSS, Balakrishna AM, Gruber G. (2013). Crystal- and NMR structures give insights into the role and dynamics of subunit F of the eukaryotic V-ATPase from Saccharomyces cerevisiae. J Biol Chem, 288(17), 11930-11939.
- Alag R, Balakrishna AM, Rajan S, Qureshi IA, Shin J, Lescar J, Grüber G, Yoon HS. (2013). Structural Insights into Substrate Binding by PvFKBP35, a Peptidylprolyl cis-trans Isomerase from the Human Malarial Parasite Plasmodium vivax. Eukaryotic Cell, 12(4), 627-634.
- Salzer R., Herzberg M., Nies D.H., Biuković G., Grüber G., Müller V., Averhoff B. (2013). The DNA uptake ATPase PilF of Thermus thermophilus: a reexamination 1 of the zinc content. Extremophiles, , 1-4.
- Ragunathan P, Biuković G, Manimekalai MSS, Lim J, Rao SPS, Grüber G. (2013). Solution structure of subunit γ (γ1-204) of the Mycobacterium tuberculosis F-ATP synthase and the unique loop of γ165-178, representing a novel TB drug target. J. Bioenerg. Biomembr, 45(1-2), 121-129.