Francisco Blanco obtained his Bachelor and Doctorate degrees in Chemistry at the Complutense University of Madrid, and did his Ph.D. thesis as supervised by J. L. Nieto at the Instituto de Estructura de la Materia (CSIC), Madrid, in 1992. As a Graduate student he used Nuclear Magnetic Resonance spectroscopy for the first characterization of linear peptides able to fold into β-hairpins in solution, providing a model system to study this structure. From 1993 - 1997 he was as a Postdoctoral Fellow at the European Molecular Biology Laboratory (EMBL, Heidelberg-Germany) in L. Serrano’s Group to study the structural properties of the spectrin SH3 domain and designed mutants, showing that the appearance of a new fold from an existing one is unlikely to occur by evolution through a route of folded intermediate sequences. In 1997 he moved to R.Tycko’s Lab at the National Institute of Diabetes, Digestive and Kidney Diseases (NIDDK, NIH, Bethesda-USA), as Visiting Fellow. Blanco applied the techniques of solid state NMR to the analysis of the HIV-Rev protein fibers, which supported a helix-loop-helix structural model. In the year 2000 he returned to Spain to work with M. Rico at the Instituto de Química Física Rocasolano (CSIC), Madrid, to participate in an international structural genomics project. The structure of a protein with unknown function revealed a possible role in cell division. He was awarded a Ramón y Cajal contract and moved to the CNIO in 2002 to lead the NMR group. He characterized the tumour suppressor ING4 as a methylated histone tail reader, novel variants of homing endonucleases as tools for gene repair, and the NMR spectrum of the PCNA ring. In december 2007 he joined the Structural Biology Unit at the CIC bioGUNE, where he works on the structural characterization of proteins and protein-protein interactions involved in cell adhesion, chromatin remodelling and DNA repair.

Dr. Blanco's Research Interets include:

• Structural Biology
• DNA Binding
• Biochemistry
• Protein Chemistry