Differences between the conformations of nitrotyrosyl-248 carboxypeptidase A in the crystalline state and in solution |
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| Authors: | James F Riordan Grazyna Muszynska |
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| Institution: | The Biophysics Research Laboratory, Department of Biological Chemistry, Harvard Medical School, Division of Medical Biology, Peter Bent Brigham Hospital, Boston, Massachusetts, USA |
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| Abstract: | In solution, nitrocarboxypeptidase A, modified at tyrosyl-248, exhibits a nitrotyrosyl pK apparent of 6.3. In the crystalline state, the pK apparent is about 8.2. This change in ionization is consistent with the hypothesis that crystallization of the enzyme causes a displacement of tyrosine-248 away from the active site zinc ion. |
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