![]() ![]() The polydispersity of the protein sample or binding of ligand or size of proteins can be characterized by using the Dynamic Light Scattering (DLS). Proteins are often associated with other proteins which lead them to form an oligomeric complex. Proteins are large bio-molecules present in their native state which perform the various biological functions. The aim of this review is to have a profound discussion on these key factors and analyze them in relation to both aspects purification and crystallization and provide a fruitful advice for boosting the production rate of protein and crystallization effectively. In this review, the key factors such as the expression system, Affinity –Tags, solubility, reducing or oxidizing environment, denaturing agents, concentration of precipitant, concentration of protein, ionic strength, isoelectric point and pH, temperature, additives, ligands, presence of substrates, coenzymes, mutation, that affect both protein purification and crystallization are discussed in detail. However, the purity and rate of crystallization success still needs to be improved. The protein solubility is achieved by the Site-directed mutagenesis that generates the hydrophobic to hydrophilic mutations. The strategies developed for protein solubility and crystallization have improved the protein production and provide high-resolution crystals for structural studies. Protein purification and crystallization problems have been noticed for many years. ![]()
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