Pressure-induced unfolding of lysozyme in aqueous guanidinium chloride solution
スポンサーリンク
概要
- 論文の詳細を見る
The pressure-induced unfolding of lysozyme was investigated in an aqueous guanidinium chloride solution by means of ultraviolet spectroscopy. Assuming a two-state transition model, volume changes were calculated from the slope of free energy vs. pressure plots over a temperature range of 10 to 60 degrees C. Between 25 and 60 degrees C, almost constant volume changes were observed in the transition region, which was reflected in almost identical slopes of the free energy change vs. pressure plots. On the other hand, the different slopes were observed in the pressure dependence of free energy change at temperatures lower than 25 degrees C. These data were interpreted as suggesting that a two-state model is not appropriate at low temperature, but instead one or more intermediates are present under these conditions. The volume changes for unfolding became less negative at temperatures higher than 25 degrees C.
- Cambridge University Pressの論文
Cambridge University Press | 論文
- Sequence analysis of porcine polymeric immunoglobulin receptor from mammary epithelial cells present in colostrum
- 土木工学のコアとは何か
- Fruit, vegetable and bean intake and mortality from cardiovascular disease among Japanese men and women : the JACC Study
- Intracellular production of adrenal renin in the fetal mouse. An immuno-electron microscopic study
- Retinol binding protein 4 in dairy cows : its presence in colostrum and alteration in plasma during fasting, inflammation, and the peripartum period