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

InhaltsangabeIntroduction.- 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.

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