Internal solvation of protein was studied by site-directed mutagenesis, with which an intrinsically fluorescent probe,tryptophan, is inserted into the desired position inside a protein molecule for ultrafast spectrosc...Internal solvation of protein was studied by site-directed mutagenesis, with which an intrinsically fluorescent probe,tryptophan, is inserted into the desired position inside a protein molecule for ultrafast spectroscopic study. Here we review this unique method for protein dynamics research. We first introduce the frontiers of protein solvation, site-directed mutagenesis, protein stability and characteristics, and the spectroscopic methods. Then we present time-resolved spectroscopic dynamics of solvation dynamics inside cavities of active sites. The studies are carried out on a globular protein, staphylococcal nuclease. The solvation at sites inside the protein molecule＇s cavities clearly reveals characteristics of the local environment. These solvation behaviors are directly correlated to enzyme activity.展开更多
介绍人型支原体(Mh)葡萄球菌蛋白 A 协同凝集试验(COA),并通过实验室操作对其主要影响因素进行了探讨,为选择最适实验条件补充提供了依据。实验研究表明,该法可测出的最低抗原蛋白浓度为0.37μg/ml。Mh 以外的多种微生物未见交叉反应。...介绍人型支原体(Mh)葡萄球菌蛋白 A 协同凝集试验(COA),并通过实验室操作对其主要影响因素进行了探讨,为选择最适实验条件补充提供了依据。实验研究表明,该法可测出的最低抗原蛋白浓度为0.37μg/ml。Mh 以外的多种微生物未见交叉反应。作者等初步认为,本法具有简易、快速、经济、特异和重复性好的优点,对 Mh 感染的快速诊断和菌种鉴定有一定应用价值。展开更多
基金Project supported by the National Basic Research Program of China(Grant Nos.2013CB921904,2009CB930504,and 2013CB328700)the National Natural Science Foundation of China(Grant Nos.11074016,11121091,10934001,61177020,11134001,and 10828407)
文摘Internal solvation of protein was studied by site-directed mutagenesis, with which an intrinsically fluorescent probe,tryptophan, is inserted into the desired position inside a protein molecule for ultrafast spectroscopic study. Here we review this unique method for protein dynamics research. We first introduce the frontiers of protein solvation, site-directed mutagenesis, protein stability and characteristics, and the spectroscopic methods. Then we present time-resolved spectroscopic dynamics of solvation dynamics inside cavities of active sites. The studies are carried out on a globular protein, staphylococcal nuclease. The solvation at sites inside the protein molecule＇s cavities clearly reveals characteristics of the local environment. These solvation behaviors are directly correlated to enzyme activity.
