Zagrobelny J A, Bright F V
Department of Chemistry, State University of New York, Buffalo 14214.
Biotechnol Prog. 1992 Sep-Oct;8(5):421-3. doi: 10.1021/bp00017a008.
The conformation of the monomeric enzyme trypsin has been studied in supercritical carbon dioxide. Steady-state fluorescence spectroscopy is used to follow the conformation of trypsin in situ as a function of CO2 density. Our results show for the first time that protein denaturation can occur during the fluid compression step and that the native trypsin is only slightly more stable (1.2 kcal/mol) than the unfolded form. These results demonstrate the power of fluorescence spectroscopy as a tool for studying protein conformation and dynamics in supercritical fluids.
已在超临界二氧化碳中研究了单体酶胰蛋白酶的构象。稳态荧光光谱法用于原位跟踪胰蛋白酶构象随二氧化碳密度的变化。我们的结果首次表明，在流体压缩步骤中可能发生蛋白质变性，并且天然胰蛋白酶仅比未折叠形式略微稳定（1.2千卡/摩尔）。这些结果证明了荧光光谱法作为研究超临界流体中蛋白质构象和动力学的工具的强大作用。
