作者: Rui Zhang , Tao Sun , Chunguang Liu , Wei Song , Zhaozhen Cao
DOI: 10.1002/JBT.21711
关键词:
摘要: n-Butanol has been widely used and its residue exists extensively in the environment. It could lead to conformational functional changes of trypsin by forming a complex with it. Docking method spectrographic technique were employed study n-butanol. The fluorescence results indicated that n-butanol can form change distance between tryptophan quenchers. proved UV-visible absorption synchronous spectroscopy indicating had little effect on conformation at low concentration while denatured coagulated high concentration. binding site was displayed molecular modeling, which gave information about distances forces trypsin. accordance spectroscopic experiments. Besides, enzyme activity assay dose-response relationship