• DOI:10.1088/1674-1056/24/1/018201
• Corpus ID: 15689536

Ultrafast solvation dynamics at internal site of staphylococcal nuclease investigated by site-directed mutagenesis

@inproceedings{Guangyu2014UltrafastSD,
  title={Ultrafast solvation dynamics at internal site of staphylococcal nuclease investigated by site-directed mutagenesis},
  author={Gao Guang-yu and Li Xiao Yu and Wang Wei and Wang Shu-feng and Dongping Zhong and Gong Qi-huang},
  year={2014}
}

• Gao Guang-yu, L. Yu, +3 authors Gong Qi-huang
• Published 9 December 2014
• Chemistry, Biology

Solvation is essential for protein activities. To study internal solvation of protein, site-directed mutagenesis is applied. Intrinsic fluorescent probe, tryptophan, is inserted into desired position inside protein molecule for ultrafast spectroscopic study. Here we review this unique method for protein dynamics researches. We 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 caves of active sites. The studies are carried out on a globular protein, staphylococcal nuclease. The solvation at internal sites of the caves indicate clear characteristics of local environment. These solvation behaviors correlated to the enzyme activity directly.