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PubMed · 14087325

METAPYROCATECHASE. I. PURIFICATION, CRYSTALLIZATION AND SOME PROPERTIES.

M NOZAKI·H KAGAMIYAMA·O HAYAISHI
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Catechol 2,3-DioxygenaseChemical PhenomenaChemistryCrystallizationOxygenasesPseudomonasResearchCHEMISTRYEXPERIMENTAL LAB STUDYOXYGENASESPSEUDOMONASJournal Article

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M NOZAKI, H KAGAMIYAMA, O HAYAISHI. 1963. METAPYROCATECHASE. I. PURIFICATION, CRYSTALLIZATION AND SOME PROPERTIES.. https://pubmed.ncbi.nlm.nih.gov/14087325/

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Thermostability of protein studied by molecular dynamics simulation.

The thermostability of protein thermostable cathechol 2,3-dixoygenase (TC23O) has been studied by the parallel molecular dynamics simulations. By analysis of the exponent beta, which is related to the scattering spectrum and constant-pressure heat capacity Cp, we reveal the respective contribution of a specific residue 228 proline; a specific salt bridge, Lys188N-Glu291OE1; four ions; and a different water environment to the thermostability of TC23O. The dynamic transition temperature of the mutants, Pro228Ser and Glu291Gly of the TC23O, was decreased about 10 degrees C and 19 degrees C respectively. The displacement of the four ions had no significant effect on the thermostability of TC23O. Water affects the thermostability by influencing the changes of accessible conformation to a certain extent. All these results agree with the known experimental results.

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