Analysis of Protein—Protein Interactions in Complex Biological Samples by MALDI TOF MS. Feasibility and Use of the Intensity-Fading (IF-) Approach

Abstract

Non-covalent macromolecular interactions is nowadays one of the most challenging fields of postgenomic biology. Genome projects have revealed that the true complexity of cellular biology exists at the level of proteins rather than at the level of genes (Pandey and Mann 2000). From the raw genetic sequences many important properties of proteins, such as three-dimensional structure, function, cellular or tissular localization or expression levels, cannot be predicted. These properties are been actively studied nowadays by proteomics approaches. Other approaches are addressing the analysis of protein-protein and protein-ligand interactions, and the derivation of protein networks (Gavin et al., 2002). The understanding of how proteins interact with each other, and with their main ligands, is an issue of fundamental interest for the comprehension of cellular functions (Alberts, 1998), as well as for the efficient application of most biomedical or biotechnological strategies based on them.