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KMID : 1059519840280010014
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Journal of the Korean Chemical Society
1984 Volume.28 No. 1 p.14 ~ p.19
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Comparision of the Pressure Denaturation of Metmyoglobin in H2O and D2O
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Kim Keon
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Abstract
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The stability difference of metmyoglobin in H2O and D2O at pH 5.7 and pH 7.0 toward pressure denaturation is studied. Metmyoglobin is denatured in D2O at smaller pressure than in H2O. The stability difference in H2O and D2O is more pronounced at pH 5.7 than at pH 7. The main reasons for the stability difference in H2O and D2O are the difference in positive charge due to H+and D+ binding to the protein in H2O and D2O, and the structural change that accompany deuteration.
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KEYWORD
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