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CrystallographicB factor of critical residues at enzyme active site

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Abstract

Thirty-seven sets of crystallographic enzyme data were selected from Protein Data Bank (PDB, 1995). The average temperature factors (B) of the critical residues at the active site and the whole molecule of those enzymes were calculated respectively. The statistical results showed that the critical residues at the active site of most of the enzymes had lowerB factors than did the whole molecules, indicating that in the crystalline state the critical residues at the active site of the natural enzymes possess more stable conformation than do the whole molecules. The flexibility of the active site during the unfolding by denaturing was also discussed.

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Bj is determined by the mass of atom and the working temperature.

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Zhang, H., Song, S. & Lin, Z. CrystallographicB factor of critical residues at enzyme active site. Sci. China Ser. C.-Life Sci. 42, 225–232 (1999). https://doi.org/10.1007/BF03183597

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Keywords

  • crystallographicB factor
  • active site
  • flexibility