Molecular Interactions and NMR
Our research uses spectroscopic methods, especially Nuclear Magnetic Resonance (NMR) spectroscopy, to probe the molecular basis of interactions between molecules.
Phone (+351) 214469300
NMR spectroscopy is a versatile experimental tool used by several groups at ITQB. Protein expression, purification and analysis provide the lab with something to study. We then use NMR to investigate molecular size and shape, as well as answer which small molecules bind to proteins, and how.
Our primary focus is on using our skills and tools to study two “neglected diseases”, cholera and tuberculosis. In the case of cholera, we are producing a safe cholera toxin in the lab and screening for functional foods that might inhibit the toxicity. Our tuberculosis project is in collaboration with Spanish and Indian collaborators and we are looking for new protein targets and drug leads. Drug-resistant tuberculosis is becoming more prevalent and our society needs new treatments.
In addition to our lab projects, we collaborate with other researchers in ITQB, Spain, Poland, France, Italy, UK and Hungary. We also improve and develop new methods to produce protein samples and conduct NMR experiments. Calcium-binding proteins, at the heart of many physiological signaling pathways, are favorites that are often used as ‘standards’ in the lab.
- J. Bandorowicz-Pikula, R. Buchet; F.J. Cańada, M. Clémancey, P. Groves, J. Jiménez-Barbero, J-M. Lancelin, O. Marcillat, S. Pikula, A. Sekrecka-Belniak, A. Strzelecka-Kiliszek “Characterization of caged compounds binding to proteins by NMR spectroscopy.” Biochem. Biophys. Res. Commun., 2010, 400, 447-451.
- P. Groves, M. Webba da Silva* “Rapid Stoichiometric Analysis of G-Quadruplexes in Solution.” Chem. Eur. J. 2010, 16, 6451-3.
- J.P. Ribeiro, M. Palczewska, S. André, F.J. Cañada, H-J. Gabius, J. Jiménez-Barbero, B. Mellström, J.R. Naranjo, D.J. Scheffers, P. Groves “Diffusion nuclear magnetic resonance spectroscopy detects substoichiometric concentrations of small molecules in protein samples.” Anal. Biochem. 2010, 396, 117-123.
Please visit the lab's website for further information