Importance Of Protein Interaction

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Protein-protein interaction can be defined as the interactions between different protein molecules within the cellular organization leading to formation of large protein complex which is modulated by non-covalent interactions such as hydrophobic interaction, hydrogen bond, van der Waals interactions etc. Protein-protein interaction plays an important role in functioning of body’s significant mechanism such as replication, transcription, translation, signal transduction, cell cycle, etc. Thus, proteins clusters together in a network map linking together various amino acids by peptide bond forming a three-dimensional structure. The entire map showing events of protein interactions that can occur in a living organism is called the interactome …show more content…
In case of proteins that undergoes interaction for a longer period resulting in permanent complex such that these interactions are strong and irreversible is called stable protein interaction. But transient protein interaction results in complex protein interaction in the oligomeric state resulting conformational change. Transient interaction can be both weak and strong. Weak transient complexes show a dynamic mixture of different oligomeric states in vivo, whereas strong transient complexes change their quaternary state only when triggered by, for example, ligand binding [3]. Hence, by understanding the characteristic of transient interface and its functioning, various protein interactions involving complex structures can be …show more content…
Some of them are pull-down assay, enzyme linked immunesorbent assay (ELISA), cross linking protein interaction analysis, etc. Pull-down assays are used for studying strong interactions using beaded support to purify interacting proteins. The main function of this technique is that it can confirm a predicted protein-protein interaction, but it can also identify novel interactions. After identification the purification consists of numerous wash and elution steps. In pull-down assays, because the specificity of the interaction is dependent on the sequence of the binding domain, these approaches are highly specific in detecting the activation of distinct proteins [2]. Another technique used for protein interaction is ELISA which can monitor protein-protein interactions in solution. ELISA assay can be performed by serial dilution of analyte in solution to check solution antigenicity and hence can perform the binding activity assessment. The advantage of ELISA technique is that it is rapid and easy to do the operation. There are three types of ELISA assay- direct, indirect and sandwich ELISA [4]. In direct ELISA antigen is attached to solid surface and antibody is directly conjugated to enzyme, in indirect ELISA the antigen is attached to solid surface but an unlabeled primary antibody first binds to the specific antigen and then an enzyme conjugated secondary antibody is attached to the primary

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