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Structural Biology Programme

Spectroscopy and Nuclear Magnetic Resonance Unit

Head of Unit:  Ramón Campos-Olivas
Research highlights

Our Core Unit incorporates a broad range of instrumentation for the biophysical characterisation of biomolecules and their interactions, including spectrophotometers, a fluorimeter, isothermal titration and differential scanning calorimeters, a circular dichrograph, dynamic and multi-angle static light scattering apparatuses, and a surface plasmon resonance (SPR) instrument. Research groups mostly from, but not limited to, the Structural Biology Programme extensively used these technologies throughout 2017. For example, in collaboration with the Cell Signalling and Adhesion Group, we conducted quantitative binding measurements using SPR (FIGURE) to establish that both the phosphatase and C2 domains of the human SHIP2 protein bind phosphatidylserine (PS) lipids, thereby most likely helping to position the active site towards its substrate. SH2-containing-inositol-5-phosphatases (SHIPs) dephosphorylate the 5-phosphate of phosphatidylinositol-3,4,5trisphosphate (PI(3,4,5)P3) and play important roles in regulating the PI3K/Akt pathway in physiology and disease.

The Unit hosts a 700 MHz NMR spectrometer that is well equipped with probes, and a sample changer for running up to 120 samples automatically. This provides the required throughput for the screening of small molecule protein binders (together with the CNIO’s Structural Biology and Experimental Therapeutics -ETP- Programmes), as well as for metabonomics measurements that, this year, were performed in collaboration with the CNIOLilly Cell Signalling Therapies Section (from the ETP), as well as the Genes, Development and Disease and the Growth Factors, Nutrients and Cancer Groups (from the Cancer Cell Biology Programme). Collectively, with these and other groups, we implemented sample preparation protocols and developed spectroscopic and analytical tools to characterise the metabolites present in different biological samples.