We are a NMR group at IRB Barcelona. We focus in two main topics:

Structure, ligand recognition and stability  of protein  domains

Intracellular communication is fundamental to the existence and survival of multi-cellular organisms and defects in this process can be a key feature of diseases such as cancer. At the molecular level, the basis for the information transfer is the formation of complex networks of interacting components.  Recent proteomic studies in yeast suggest that at least 70% of tested proteins assemble in multi-component complexes that underlines the central position of protein: protein interactions in the survival of eukaryotic organisms.

Protein domains are discrete structural and functional units that have been shuffled and reorganized throughout the course of evolution and are a common feature of proteins from multicellular organisms. Due to their relative small size and compact fold, protein domains are very amenable to structural studies, in particular in solution by Nuclear Magnetic Resonance, which is the technique used in our laboratory. We are interested in the identification of the rules that govern specificity and selectivity of a given type of domain inside an organism and in several organisms

Automated assignment of NMR spectra

The last decade has seen an upsurge in the popularity and success of NMR for structural studies of proteins in solution. Protein expression using 15 N and 13 C labeling is now technically and economically affordable for most labs and it has opened a new avenue in NMR since it allows the use of triple resonance experiments as a rutine. The combination of these experiments together with residual dipolar couplings has greatly increased the quality of NMR data and thus the quality of the structures determined by NMR.

The main bottle-neck of the NMR process still lies at the data-analysis step, called resonance assignment. We are working on a programme package that combines peak-picking and assignment

processes , giving a better performance in both tasks and reducing the user-intervention drastically and  assigning not only protein backbone and carbon side-chains but also protons in an automated manner .

It is clear that high-throughput studies in structural or fuctional genomics by NMR rely on the availability of automation of data acquisition and analysis, ideally requiring a limited human contribution. We are working on a programme package that combines peak-picking and assignment processes, giving a better performance in both tasks and reducing the user-intervention drastically. In addition, the package we are developing is going to assign not only protein backbone and carbon side-chains but also  aliphatic sidechain protons in an automated manner.