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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.

Biochemistry. --- Computational biology. --- Life sciences. --- Xylanases -- Biotechnology. --- Computational biology --- Xylanases --- Proteins --- Fungi --- Protein Stability --- Technology, Pharmaceutical --- Glycoside Hydrolases --- Investigative Techniques --- Eukaryota --- Hydrolases --- Amino Acids, Peptides, and Proteins --- Biochemical Phenomena --- Enzymes --- Organisms --- Analytical, Diagnostic and Therapeutic Techniques and Equipment --- Chemical Phenomena --- Chemicals and Drugs --- Enzymes and Coenzymes --- Phenomena and Processes --- Ascomycota --- Fungal Proteins --- Enzyme Stability --- Xylosidases --- Human Anatomy & Physiology --- Biology --- Health & Biological Sciences --- Biology - General --- Animal Biochemistry --- Biotechnology --- Xylanases. --- Analysis. --- Structure-activity relationships. --- Endoxylanases --- Xylan endoxylosidases --- Proteids --- Proteins. --- Enzymology. --- Bioinformatics. --- Life Sciences. --- Protein Science. --- Bio-informatics --- Biological informatics --- Information science --- Systems biology --- Biochemistry --- Biomolecules --- Polypeptides --- Proteomics --- Biosciences --- Sciences, Life --- Science --- Data processing --- Glycosidases --- Enzymes. --- Biocatalysts --- Ferments --- Soluble ferments --- Catalysts --- Enzymology --- Biological chemistry --- Chemical composition of organisms --- Physiological chemistry --- Chemistry --- Medical sciences --- Composition --- Proteins .