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  • Analysis of the critical sites for protein thermostabilization by . . .
    To identify the critical sites for protein thermostabilization by proline substitution, the gene for oligo-1,6- glucosidase from a thermophilic Bacillus coagulans strain, ATCC 7050, was cloned as a 2 4-kb DNA fragment and sequenced In spite of a
  • Analysis of the critical sites for protein thermostabilization by . . .
    To identify the critical sites for protein thermostabilization by proline substitution, the gene for oligo-1,6- glucosidase from a thermophilic Bacillus coagulans strain, ATCC 7050, was cloned as a 2 4-kb DNA fragment and sequenced In spite of a big difference in their thermostabilities, B coagulans oligo-1,6-glucosidase had a large number of points in its primary structure identical to
  • Analysis of the critical sites for protein thermostabilization by . . .
    Analysis of the critical sites for protein thermostabilization by proline substitution in oligo-1,6-glucosidase from Bacillus coagulans ATCC 7050 and the evolutionary consideration of proline residues
  • Protein thermostabilization by proline substitutions - ScienceDirect
    We have generated several lines of evidence supporting the theory from the comparative analysis of oligo-1,6-glucosidases in their primary and secondary structures and molecular properties, the X-ray crystal structure analysis of the Bacillus cereus oligo-1,6-glucosidase, and the enhancement in thermostability of the oligo-1,6-glucosidase by
  • Analysis of the critical sites for protein thermostabilization by . . .
    In spite of a big difference in their thermostabilities, B coagulans oligo-1,6-glucosidase had a large number of points in its primary structure identical to respective points in the same enzymes from a mesophilic Bacillus cereus strain, ATCC 7064 (57%), and an obligately thermophilic Bacillus thermoglucosidasius strain, KP1006 (59%)
  • RCSB PDB - 1UOK: CRYSTAL STRUCTURE OF B. CEREUS OLIGO-1,6-GLUCOSIDASE
    The refined structure reveals the locations of 21 proline-substitution sites that are expected to be critical to protein thermostabilization from a sequence comparison among three Bacillus oligo-1,6-glucosidases with different thermostability
  • Multiple Proline Substitutions Cumulatively Thermostabilize Bacillus . . .
    The resultant nine active mutant enzymes contained 1–9 more proline residues than B cereus oligo-1,6-glucosidase The thermostability of these mutants was additively enhanced with the increase in the number of proline residues introduced





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