Experimental techniques to study protein-DNA interaction are classified into two forms, namely in vitro and in vivo. In vivo studies are useful due to the preservation of the natural structure of the interaction sides. However, in multiprotein proteins, it is difficult to determine which part of the protein is directly connected to and protects DNA. In contrast, in vitro study is suitable for purified proteins and protein subunits. Say no to plagiarism. Get a tailor-made essay on “Why violent video games should not be banned”?Get the original essayIn the late 1960s, the first studies were carried out on DNA-protein interaction. Binding tests on nitrocellulose filters were the first technique proposed for this purpose. In the 1990s, many diverse experimental techniques were developed to study DNA-protein interaction. Nowadays, many techniques are available for the detection and characterization of protein-nucleic acid complexes and most have advantages and disadvantages. Such techniques include, but are not limited to, electrophoretic mobility shift assays (EMSA) (Fried 1989), DNase I fingerprinting (Brenowitz et al. 1986), bacterial mono-hybrid system, and techniques based on chromatin immunoprecipitation (ChIP) analysis, e.g. immunoprecipitation of chromatin with DNA. microarray (ChIP-chip; Lieb et al. 2001), chromatin immunoprecipitation sequencing (ChIP-Seq; Johnson et al. 2007), ChIP-exo (Pugh 2012), and chromatin immunoprecipitation tags (ChIP-PET ; Wu et al. 2013) were used. Many techniques are available for the detection and characterization of protein-nucleic acid complexes and most have advantages and disadvantages for the determination and characterization of the DNA-protein relationship. Electrophoretic mobility shift assays (EMSA); Electrophoretic mobility shift assays (also known as "band shift assays" and "mobility shift electrophoresis") feature a standard protocol for studying a wide range of nucleic acid-protein interactions, since single protein binding events to the assembly of large complexes such as the spliceosome. (Malloy 2000; Rio 2014). The EMSA technique was initially introduced by Fried 1989 and nowadays many variants have been described in the literature. EMSA is a simple, rapid, and highly sensitive laboratory technique for qualitatively testing specific interactions between nucleic acids and proteins, although, under appropriate conditions, it is used for quantitative purposes. However, EMSA is not without limitations and greater limitations and problems have been encountered (Hellman and Fried 2007). This technique is based on the observation that the binding segments of the nucleic acid to the protein cause a decrease in the electrophoretic mobility of the segment relative to the free nucleic acid in the agarose gel in the native state or in non-denaturing polyacrylamide gel (Vinckevicius and Chakravarti, 2012; Rio 2014). In this technique, a mixture of crude proteins or purified proteins are mixed with the nucleic acid sequence in a suitable buffer and specific binding can occur, stable complexes of nucleic acid and protein (the probe can be bound nonspecifically by other proteins) were separated. by non-denaturing gel electrophoresis; not only for the study of nucleic acid sequence binding requirements, but also various aspects.