Appendix - CNIC

SCIENTIFIC REPORT ´09 7 Technical Units
Proteomics
> RESEARCH INTEREST
Head of Unit: Juan Antonio López
Research Scientists: Enrique Calvo
Emilio Camafeita
The Proteomics Unit provides technical expertise in several
proteomics approaches for the separation, quantification,
identification and characterization of proteins in biological
systems, and maintains programs to develop and improve
technologies and protocols to meet the demands of the
research community. The Unit has a complete system for the
separation and quantitative analysis of differential protein
expression by 2D-DIGE as well as systems for gel-free
separation based on multidimensional nanoHPLC. Proteins are
identified using MALDI-TOF/TOF and ESI mass spectrometers,
the latter comprising a hybrid triple quadrupole (TQ) and a
linear ion trap coupled to an Orbitrap high resolution mass
analyzer. The high resolution and scanning speed of the
Orbitrap mass spectrometer enables optimal characterization
of proteomes and subproteomes, while the specific scanning
modes of the TQ allow sensitive targeted analysis of proteins
and posttranslational modifications.
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This robust and comprehensive analytical platform enables us
to take on large and technically demanding research projects
that require both qualitative and quantitative proteomic
approaches for the detection of differential protein expression,
chemical and posttranslational modifications, and proteinprotein
interactions in diverse biological systems. The Unit
maintains close collaborations with other laboratories to
investigate new approaches for the selective analysis of
specific subproteomes and interactomes.
Last year, the Unit’s recognized expertise in the field was
reflected in the award to a member of the Unit (E. Calvo) of
the Sociedad Española de Proteómica prize for the best
proteomics paper of 2007-2008. This paper was published in
Nature Chemical Biology (3, 117-125; 2007) and was
featured on the journal cover.
Identification of nitrosylated Cys residues in
peptides. Fragmentation spectra from Cys76unmodified
(top) and Cys76-nitrosylated
(bottom) Kir2.1 tryptic peptide. From Gómez
et al.