Entropic stabilization of the tryptophan synthase α-subunit from a hyperthermophile, Pyrococcus furiosus : X-ray analysis and calorimetry

This research was originally published in Journal of Biological Chemistry. Yuriko Yamagata, Kyoko Ogasahara, Yusaku Hioki, Soo Jae Lee, Atsushi Nakagawa, Haruki Nakamura, Masami Ishida, Seiki Kuramitsui, and Katsuhide Yutani. Entropic stabilization of the tryptophan synthase α-subunit from a hyperthermophile, Pyrococcus furiosus : X-ray analysis and calorimetry. J. Biol. Chem. 2001; 276, 11062-11071. © the American Society for Biochemistry and Molecular Biology

Absence of the thermal transition in apo-α-lactalbumin in the molten globule state : A study by differential scanning microcalorimetry

To estimate the energy level of the molten globule state, the heat capacity function of apo-α-lactalbumin in the molten globule state has been examined using a scanning microcalorimeter at neutral pH. The results showed that the enthalpy difference between the molten globule state and presumed unfolded state by heating was almost zero at neutral pH, demonstrating that the molten globule state does not exhibit any co-operative transition upon heating. This is in agreement with the results already reported at acid pH, but is apparently in conflict with that recently reported with some assumptions at neutral pH

Light scattering can detect the thermal-dependent conformational changes of proteins

New methods and tools (I), Poster Session, Abstract, Meeting Program of EABS & BSJ 200

Structure of Physarum polycephalum cytochrome b 5 reductase at 1.56 Å resolution

The structure of P. polycephalum cytochrome b 5 reductase, an enzyme which catalyzes the reduction of cytochrome b 5 by NADH, was determined at a resolution of 1.56 Å