Pressure-temperature-induced denaturation of yeast phosphoglycerate kinase, a double-domain protein.
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.
Tanaka
T
T
Department of Polymer Science and Engineering, Kyoto Institute of Technology, Matsugasaki, Sakyo, Kyoto, Japan.
Ikeuchi
H
H
Tanaka
N
N
Kunugi
S
S
D044367:Phase Transition; D010735:Phosphoglycerate Kinase / Q000737:chemistry*; D011312:Pressure; D011489:Protein Denaturation; D017434:Protein Structure, Tertiary; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D013057:Spectrum Analysis; D013696:Temperature; D013816:Thermodynamics
D029701:Saccharomyces cerevisiae Proteins; D010735:Phosphoglycerate Kinase