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Information Seminar Paper

Title

PREDICTION OF RESIDUE PAIRS FOR STABILIZING DISULFIDE MUTATION

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 Start Page | End Page

Abstract

 IN PROTEIN ENGINEERING AND DESIGN, ENHANCING THE STABILITY OF PROTEINS IS OF GREAT INTEREST IN BOTH BASIC RESEARCH AND INDUSTRIAL APPLICATIONS. OWING TO THE ECONOMIC BENEFIT OF APPLYING A THERMOZYME IN AN INDUSTRIAL PROCESS, MANY STRATEGIES FOR RATIONAL PROTEIN STABILIZATION HAVE BEEN SUGGESTED. DISULFIDE ENGINEERING AS ONE OF THESE APPROACHES HAS BECOME A POWERFUL EXPERIMENTAL MODIFICATION TOOL TO ALTER PROTEIN STABILITY. MOREOVER, NOVEL DISULFIDE BONDS HAVE BEEN USEFUL FOR COMPREHENSION OF PROTEIN CONFORMATION, DYNAMICS AND FUNCTION. RECENT STUDIES SUGGEST THAT INCLUSION OF STRUCTURAL FEATURES IN DISULFIDE ENGINEERING WOULD IMPROVE THE LIKELIHOOD OF A STABILIZING MUTATION. IT IS DESIRABLE TO CHOOSE RESIDUE PAIRS THAT ARE IN RELATIVELY FLEXIBLE REGIONS CLOSE TO THE PROTEIN SURFACE. IN THIS ARTICLE, THE SOFTWARE PROTEIN DISULFIDE MUTANT PROPOSER HAS BEEN INTRODUCED. THE SOFTWARE CAN PROPOSE PAIRS OF RESIDUES BASED ON CB-CB/CA-CA DISTANCE, RESIDUE ACCESSIBILITY, TEMPERATURE FACTOR AND CHANGE IN VOLUME UPON MUTATION THAT WILL PROBABLY FORM A DISULFIDE BOND AND IMPROVE THERMOSTABILITY OF PROTEIN IF MUTATED TO CYSTEINE. THE SOFTWARE IS FREELY AVAILABLE AT HTTP: //BIOINF.MODARES.AC.IR/SOFTWARE/DESIGNER/.

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