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

One of the first reports showing stable, energy efficient model towards improved protein function prediction screening in-silico structure based mutagenesis of xylanases from Thermomyces lanuginosus Discusses computational strategies towards improved protein function prophecy and insilico structure based mutagenesis of xylanases from Thermomyces lanuginosus Describes the computational design of family 11 xylanase (endo-1,4-ß-xylanase) from Thermomyces lanuginosus Includes supplementary material: sn.pub/extras Includes supplementary material: sn.pub/extras

Inhalt
Introduction.- Material and Methods.- Selection of sequences, 3D structures and multiple sequence alignment.- Mutant generation.- Energy minimization.- Stereo-chemical quality check and analysis of non-bonded interactions.- Protein-protein docking.- InterProScan.- Identification of functionally important regions of wild type viz. Endo-1, 4-beta xylanases (1YNA).- 3d2GO server: From protein 3D structure to Gene Ontology (GO) term.- Results and discussions.- Conclusion.