Computational Strategies Towards Improved Protein Function Prophecy of Xylanases from Thermomyces lanuginosus
This Brief reports on the interplay of an amino-acid mutation towards substrate which could lead to enhanced effects on mutant. These effects need to be given consideration in the engineering processes of protein stability and further exploration of such learning are required to provide novel indication for selection of an enzymes. There are very few reports showing such stable, energy efficient model towards improved protein function prediction screening in-silico structure based mutagenesis of xylanases from Thermomyces lanuginosus
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19 mutants 1YNA 2D representation 3D Structure amino acids atoms benchmark binding site binding sites Bioinformatics biological Camacho Computational design conformational changes data set docking algorithm docking approaches docking methods family 11 xylanases Gene Ontology Glycoside hydrolase grid points identification of functionally identify Improved Protein Function interacting with xylan interaction sites InterProScan Laskowski ligand M. V. K. Karthik Molecular docking molecular dynamics molecule multiple sequence alignment mutant is represented Mutant residue interacting near-native pocket PROCHECK Prophecy of Xylanases protein complexes protein design protein docking protein domains Protein Function Prophecy protein interactions protein structures protein surface protein–protein docking protein–protein interactions proteolysis Ramachandran plot representation of binding Representation of mutant represented in yellow rigid-body docking RMSD scoring function sequence side-chain solvent SpringerBriefs in Systems Strategies Towards Improved support vector machines surface patches Systems Biology target Thermomyces lanuginosus unbound structures wild type xylan Xylanases from Thermomyces xylobiose and beta-D-xylopyranose