Pressure-temperature-induced denaturation of yeast phosphoglycerate kinase, a double-domain protein. |
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Authors: | T Tanaka H Ikeuchi N Tanaka S Kunugi |
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Institution: | Department of Polymer Science and Engineering, Kyoto Institute of Technology, Matsugasaki, Sakyo, Kyoto, Japan. |
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Abstract: | Pressure-induced denaturation of yeast phosphoglycerate kinase was studied at various temperatures, as a model double-domain protein, using intrinsic fluorescence, 4th derivative absorbance, CD, and DSC. A thermodynamic transition intermediate was observed in the pressure-denaturation, as was reported for the cold denaturation. From the different response of Trp and Tyr residues, as monitored by fluorescence and 4th derivative absorbance changes, the C-terminal domain carrying all the Trp residues seemed to exert structural changes at relatively lower pressure. A further structural change involving both domains was observed at higher pressures. The two-step changes occurred almost simultaneously during heat denaturation. |
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