Head


Matthias Görlach
Matthias Görlach

Staff Scientists

Oliver Ohlenschläger

Ramadurai Ramachandran

PhD Students

Peter Bellstedt

Yvonne Ihle

André Mischo

Thomas Seiboth

Christoph Wiedemann

Diploma Students

Sebastian Haumann

Henriette Kutscha

Technicians / Engineers

Sabine Häfner

Angelika Heller

Christiane Hirsch (secretary)

Jörg Leppert (NMR hardware)



 

Görlach Laboratory

Biomolecular NMR spectroscopy

Structural basis of biomolecular interactions in aging and disease

zinc-binding methionine sulfoxide reductase

Metabolic and regulatory processes critically depend upon specific biomolecular recognition mechanisms. Disturbance of specific recognition may lead to loss of recognition fidelity or derailment of biological processes and thus to the development of acute or chronic disease. Proper recognition depends on "fitting" contact surfaces of the interacting biomolecules. We are employing heteronuclear NMR spectroscopy in the liquid and the solid state to investigate the structure of biomolecules and their interactions, in order to shed light on their structure-function relationship. This should contribute to understanding the molecular mechanisms relevant to ageing and to the pathogenesis of age-related diseases.

 

» Structure of a zinc-binding methionine sulfoxide reductase [PDB | JenaLib]

 

 

 

Projects

The systems we are working on include proteins involved in maintenance of the genome and in repairing DNA and oxidative protein damage, papillomaviral oncoproteins, and aggregates of proteins contributing to papillomavirus release and the pathogenesis of Alzheimer's disease. In this context, we are also engaged in developing techniques for solid state NMR, which is a powerful tool for the structural characterisation of biomolecules not amenable to investigation by solution state NMR or X-ray crystallography.

 

Recent selected publications

  • Haupt C, Leppert J, Rönnike R, Meinhardt J, Yadav JK, Ramachandran R, Ohlenschläger O, Reymann KG, Görlach M, Fändrich M (2011) Oligomer structure provides a basis for preventing Aß-dependent synaptic dysfunctions. Angew Chem Int Ed Engl, accepted for publication
  • Carella M, Becher J, Ohlenschläger O, Ramachandran R, Gührs KH, Wellenreuther G, Meyer-Klaucke W, Heinemann SH, Görlach M (2011) Structure-function relationship in an archaebacterial methionine sulphoxide reductase B. Mol Microbiol 79, 342-358. [PubMed] [PDB code: 2K8D]
  • Tietze D, Voigt S, Mollenhauer D, Tischler M, Imhof D, Gutmann T, González L, Ohlenschläger O, Breitzke H, Görlach M, Buntkowsky G (2011) Revealing the position of the substrate in nickel superoxide dismutase: a model study. Angew Chem Int Ed Engl 50, 2946-2950. [PubMed]
  • Duchardt-Ferner E, Weigand JE, Ohlenschläger O, Schmidtke SR, Suess B, Wöhnert J (2010) Highly modular structure and ligand binding by conformational capture in a minimalistic riboswitch. Angew Chem Int Ed Engl 49, 6216-6219. [PubMed]
  • Schwalbe M, Ohlenschläger O, Marchanka A, Ramachandran R, Häfner S, Heise T, Görlach M (2008) Solution structure of stem-loop alpha of the hepatitis B virus post-transcriptional regulatory element. Nucleic Acids Res, 36, 1681-1689. [PubMed; PDB code: 2JYM]
  • Riedel K, Herbst C, Häfner S, Leppert J, Ohlenschläger O, Swanson MS, Görlach M, Ramachandran R (2006) Constraints on the structure of (CUG)97-RNA from magic-angle-spinning solid-state NMR spectroscopy. Angew Chem Int Ed Engl, 45, 5620-5623. [PubMed]
  • Ohlenschläger O, Seiboth T, Zengerling H, Briese L, Marchanka A, Ramachandran R, Baum M, Korbas M, Meyer-Klaucke W, Dürst M, Görlach M (2006) Solution structure of the partially folded high-risk human papilloma virus 45 oncoprotein E7. Oncogene, 25, 5953-5959. [PubMed; PDB code: 2F8B]

 

Current job offers

Students interested in a PhD thesis in NMR / structural biology and within the framework of the Leibniz Graduate School of Aging and Age-Related Diseases (LGSA) are encouraged to apply. Further information can be found here.

 

Last update: October 21, 2011
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