The ultimate goal of protein modeling is to predict a structure from its sequence with accuracy equivalent to the best experimentally obtained results. In all contexts where today only experimental structures provide solid foundations, it would allow users to use quickly in-silico protein models safely: structural drug design, protein function analysis, interacting, antigenic behaviors and the rational conception of proteins with increased stability or novel functions. Moreover, protein models can only be obtained if experimental techniques fail. Many proteins are just too large for an NMR test, and for X-ray diffraction they can't crystallize. In cases where there are difficulty in obtaining experimental structures for a given protein, the comparative modeling of protein structures offers an efficient alternative to determining experimental structure. Normally a model with an estimated RMSD of 1 to 4 to the experimental structure may be obtained if you find a structural template that is more than 50% identical to the query sequence.
Cite this article:
Akshay R. Yadav, Shrinivas K. Mohite. Homology Modeling and Generation of 3D-structure of Protein. Res. J. Pharma. Dosage Forms and Tech.2020; 12(4):313-320. doi: 10.5958/0975-4377.2020.00052.X
Akshay R. Yadav, Shrinivas K. Mohite. Homology Modeling and Generation of 3D-structure of Protein. Res. J. Pharma. Dosage Forms and Tech.2020; 12(4):313-320. doi: 10.5958/0975-4377.2020.00052.X Available on: https://rjpdft.com/AbstractView.aspx?PID=2020-12-4-14
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