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Mutagenesis

Description: This procedure allows you to compare the binding activity (IC50) for a protein and its mutated form regarding a known ligand. The Quantum technology provides interface for changing protein sequences at specific sites through alterations to its amino acids to apply molecular modeling techniques to predict properties of mutated structures. The result of calculations is the information about the coordinates of the docked ligands to native and mutated structures and the corresponded affinity constants (IC50). It gives accurate prediction of changes in bioactivity of mutated form of protein. The Quantum technology is also irreplaceable for computational estimation of alterations in receptor recognition connected with protein mutations, as well as for prediction of changes in protein-protein interactions and corresponding changes in metabolic, disease and other pathways. The accurate assessment of mutated proteins activity is also necessary for elaborating strategy for protein engineering and directed mutagenesis, as well as for drug resistance research. The in-silico mutated form of protein can also be used for virtual screening, study of conformational changes, protein-protein interactions research and all other types of research available with Quantum technology.

Requirements: It is necessary to have the 3D structure of a protein, and the 2D or 3D structure of a ligand. The position of the active site of the protein should be known. The protein and the ligand structures should be uploaded with a standard format. (.pdb, .hin, .mol2 etc.). The ligand has to have not more then 25 flexible bonds.

Output/Results:

You will receive .pdb files with coordinates of the docked ligands to native and mutated structures and the corresponded affinity constants.

Accuracy of the prediction: Absolute deviation – 8 kJ and relative deviation – 15% (see Proof of consept_IC50).

Upload necessary information.

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