<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Gao, G.</style></author><author><style face="normal" font="default" size="100%">Y. Li</style></author><author><style face="normal" font="default" size="100%">Wang, W.</style></author><author><style face="normal" font="default" size="100%">Zhong, D.</style></author><author><style face="normal" font="default" size="100%">S. Wang</style></author><author><style face="normal" font="default" size="100%">Gong, Q.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Picosecond time-resolved fluorescent spectroscopy of 1-anilino-8-naphthalene sulfonate binding with staphylococcal nuclease in the native and molten globule states</style></title><secondary-title><style face="normal" font="default" size="100%">J Photochem Photobiol BJ Photochem Photobiol BJ Photochem Photobiol B</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Journal of photochemistry and photobiology. B, Biology</style></alt-title><short-title><style face="normal" font="default" size="100%">Journal of photochemistry and photobiology. B, BiologyJournal of photochemistry and photobiology. B, Biology</style></short-title></titles><dates><year><style  face="normal" font="default" size="100%">2015</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Apr</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">145</style></volume><pages><style face="normal" font="default" size="100%">60-5</style></pages><isbn><style face="normal" font="default" size="100%">1873-2682 (Electronic)1011-1344 (Linking)</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">We studied the picosecond time-resolved fluorescent spectroscopy of 1-anilino-8-naphthalene sulfonate (ANS), which binds to the staphylococcal nuclease (SNase) of the wild-type (WT) and the molten globule (MG) state. Three ANS emission bands at approximately 530nm, approximately 495nm, and approximately 475nm are resolved, corresponding to three ANS states: the free ANS in solution and associated form adsorbing to surface sites and binding to active sites. The surface hydrophobicity of the WT is moderate and different from the MG state, as shown both in the position of the bands and by the concentration dependent ANS fluorescent decay. For MG, the decay of two blue bands accelerated with the increment of the ANS concentration, whereas the WT did not show this dependency. However, when pdTp, an inhibitor, was attached to the active site of the MG state, band 2 decay was also independent of the ANS concentration. These results indicate that the protein hydrophobic sites have two types of interactions with ANS.</style></abstract><accession-num><style face="normal" font="default" size="100%">25771383</style></accession-num><notes><style face="normal" font="default" size="100%">Gao, GuangyuLi, YuWang, WeiZhong, DongpingWang, ShufengGong, QihuangengResearch Support, Non-U.S. Gov'tSwitzerland2015/03/17 06:00J Photochem Photobiol B. 2015 Apr;145:60-5. doi: 10.1016/j.jphotobiol.2015.02.018. Epub 2015 Mar 3.</style></notes><auth-address><style face="normal" font="default" size="100%">Institute of Modern Optics, State Key Laboratory for Artificial Microstructure and Mesoscopic Physics, School of Physics, Peking University, Beijing 100871, China.Department of Physics, Department of Chemistry and Biochemistry, and Programs of Biophysics, Chemical Physics and Biochemistry, The Ohio State University, Columbus, OH 43210, USA. Electronic address: zhong28@osu.edu.Institute of Modern Optics, State Key Laboratory for Artificial Microstructure and Mesoscopic Physics, School of Physics, Peking University, Beijing 100871, China. Electronic address: wangsf@pku.edu.cn.</style></auth-address></record></records></xml>