Protein-protein interactions are located in the heart of most cellular processes including carbohydrate and lipid metabolism, cell cycle regulation, protein and nucleic acid metabolism, signal transduction and cellular architecture. A comprehensive understanding of the cellular function depends on a full characterization of the complex network of cellular protein-protein Association.
Experimental methods
1. Yeast two-hybrid system.
2. Affinity chromatography.
3. DIPTM database.
1. Yeast two-hybrid system:
This is the most commonly used technology for protein-protein interaction. Many new protein interactions were discovered by this method. The method can characterize interactions only Bimolekulare.
2. Affinity chromatography:
This is a protein separation method using specific binding interactions that occur between molecules.
3. DIPTM database:
This is a database of interacting proteins and catalogues experimental interactions between proteins. It combines to create information from a variety of sources in a single uniform set of protein-protein interactions.
Inferring protein-protein interactions not homology methods
Computer-aided methods assign usually protein function sequence similarity approach. The non-homology strategy not to sequence similarity down. Instead, the strategy is to group proteins, which are part of the same way and define them as a functionally connected.
The non-homology approaches are;
1. Domain-merger analysis.
2. Correlated messenger RNA expression pattern.
3. Phylogenetic profiles.
1. Domain-Fusion:
This strategy two non-homologous components be found consisting of separately in a different genome fusion protein. Such components will interact expected to physically with each other. An interface between two component is interacting more likely to develop when the proteins in a single chain are fused. In some respects, the domain-merger analysis is similar to the use of gene cluster for functional links from gene close to derive.
2. Correlated messenger RNA expression pattern:
This analysis is based on the premise that proteins with correlated level compared to the same series are functionally linked to conditions. The functional annotations are typically broad, with features such as 'Metabolism' or 'Transcription' specified. Even a random pair of proteins has a chance of 50% of the similar function widely. However, since the comments generally by a number of connections are derived, much more than random informative they are links similar interactions, in the best case, experimental determination of protein-protein.
3. Phylogenetic profiles:
Phylogenetic profiling is based on the correlated evolution of proteins. If they release a phylogenetic profile, which is defined over a set of genomes, as the pattern of protein deposits, the development of two proteins is correlated. The phylogenetic profile can be calculated exactly only comparing multiple complete genome. Two proteins that share a similar phylogenetic profile are functionally connected. So, clusters of proteins, which can be based on their phylogenetic profiles provide information about the function of uncharacterized protein that are grouped with one or more functionally defined proteins.
Conclusion
The protein-protein interactions that are very important for most cellular studies of experimental or not homology methods can be detected. So are the basis for the next step in protein studies, such as drug discovery.
Suganya Raphael is founder of Zion business solutions, a Biotechnologist and a know-how in the field of life science. It is also a creative and talented editor with computer knowledge. It is a M.Phil in biotechnology and Castle with a master's degree in biotechnology and Bachelor's degree in microbiology. She has previously worked as a lecturer. She is also adept at social media marketing, blogging, development of content and writing articles.
