> Bacterial disease
> Calcium-binding proteins
> G-quadruplexes
> New methods





Recent publications from the lab

O. Reinstein, M.A.D. Neves, M. Saad, S.N. Boodram, S. Lombardo, S.A. Beckham, J. Brouwer, G.F. Audette, P. Groves, M.C.J. Wilce and P.E. Johnson “Thermodynamic and Hydrodynamic Analysis of Steroid Binding by an Engineered Aptamer”, Biochemistry, accepted for publication.

DNA aptamer structures provide a flexible scoffold for the specific detection of molecules. The change in size and shape that occurs on binding can be exploited as a switch to detect low levels of, in this case, steroids similar to cocaine. Patrick collected DOSY data on supplied DNA and DNA complex samples to corroborate data obtained from other methods.

A. Cmoch, A. Strzelecka-Kiliszek, M. Palczewska, P. Groves and S. Pikula “Matrix vesicles isolated from mineralization-competent Saos-2 cells are selectively enriched with annexins and S100 proteins” Biochem. Biophys. Res. Commun. 2011, 412 , 683-697.
Annexins play an essential role in matrix vesicle function.
S100s are important modulators of annexins. This is the first report that S100 EF-hand proteins are present in matrix vesicles and that the protein levels of annexins and S100s change upon stimulation of the mineralization process.

M. Palczewska, I. Casafont, K. Ghimire, A.M. Rojas, A. Valencia, M. Lafarga, B. Mellström, J.R. Naranjo "Sumoylation regulates nuclear localization of repressor DREAM" Biochim Biophys Acta. 2011, 1813, 1050-1058.
How an EF-hand protein, called DREAM, can enter the nucleus.


M. Kowacz, P. Groves, J. Esperança, L.P. Rebelo “On the use of ionic liquids to tune crystallizationCrystal Growth & Design, 2011, 11, 684-691.
New chemicals and approaches to crystallizing proteins. Patrick collected DOSY data to help with the characterization of the chemical properties with this ITQB collaboration.


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.
Caged compounds provide useful tools for biochemical studies but we assume the caged compounds do not bind to the protein to start with or affect the results. We used STD to show this is not the case. This project started when I was in Spain, with French and Polish collaboraters, and ended in Portugal.


P. Groves*, M. Webba da Silva* “Rapid Stoichiometric Analysis of G-Quadruplexes in Solution.” Chem. Eur. J. 2010, 16, 6451-3.
DOSY was used to characterize G-Quadruplexes for the first time. The project was first discussed in the UK with DOSY data collected and analyzed by Patrick in Portugal.


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.
Another project initiated when Patrick was in Spain. We developed a DOSY protocol to detect contamination of small molecules in protein solutions. The proteins were produced in our lab, Spain and Germany with the NMR protocols developed in Portugal verified by a Spanish lab.