[Zurück]

P. Lanzendorfer, D. Borgmann, A. Steininger, S. Schaller, M. Brameshuber, S. Sunzenauer, G. Schütz, O. Höglinger, S. Winkler, J. Weghuber:
"Analysis of Protein-Protein Interactions in Live Cells - The Micro-Patterning Approach";
in: "Protein Purification and Analysis - Methods and Applications. iConcept press 2013", iConcept Press Ltd., 2013, ISBN: 978-1-477555-05-7, S. 1 - 32.

Proteins are key-players that enable most biological processes in a cell, among them cell growth and proliferation, gene expression, inter and intracellular communication, cell morphology and motility. The study of protein functions is complex with many critical aspects including the expression profile, post-translational modifications, a distinct intracellular localization as well as interactions with other proteins (Golemis, 2005).
Protein-protein interactions (PPIs) occur when two or more proteins bind together. In most cases these binding processes are necessary for the biological function of the protein. The nature of PPIs can be characterized as stable or transient, and both interaction types can be either strong or weak, fast or slow. The interactions of proteins that can be purified as multi-subunit complexes are defined as stable interactions. For example, hemoglobin forms a stable complex by multi-subunit interaction (Bucci et al., 1965). Other well-known examples include more complicated assemblies of polypeptides, including metabolic enzymes, the DNA-replication complex or the nuclear pore complex. In many cases their activity is associated with large structures termed protein machines (Alberts & Miake-Lye, 1992).