西亚试剂：Tuning the Electronic Absorption of Protein-Embedded All-tr

Tuning the Electronic Absorption of Protein-Embedded All-trans-Retinal

Wenjing Wang, Zahra Nossoni, Tetyana Berbasova, Camille T. Watson, Ipek Yapici, Kin Sing Stephen Lee, Chrysoula Vasileiou, James H. Geiger*, Babak Borhan*

Protein-chromophore interactions are a central component of a wide variety of critical biological processes such as color vision and photosynthesis. To understand the fundamental elements that contribute to spectral tuning of a chromophore inside the protein cavity, we redesigned human cellular retinol binding protein II (hCRBPII) to fully encapsulate all-trans-retinal and form a covalent bond as a protonated Schiff base. This system, using rational mutagenesis designed to alter the electrostatic environment within the binding pocket of the host protein, enabled regulation of the absorption maximum of the pigment in the range of 425 to 644 nanometers. With only nine point mutations, the hCRBPII mutants induced a systematic shift in the absorption profile of all-trans-retinal of more than 200 nanometers across the visible spectrum

• 以上资料由西亚试剂：http://www.xiyashiji.com/ 提供此产品的详细信息如密度,含量,分子式,分子量等均可在西亚官网查询   
• 相关产品如诺卡氏菌液(-)-樟脑神经鞘磷脂,从牛脑所得 杨梅苷愈创奥IAPN-叔丁基苯硫腈氯化物4-溴苯基五氟化硫色胺盐酸盐4-溴噻吩-2-甲醛纤维素粉 7-(二甲基氨基)-4-三氟甲基香豆素邻硝基苯肼盐酸盐3,3'-二氨基联苯胺四盐酸盐水合物美伐他汀丁卡因阿卡明全氟辛基季胺碘化物布西拉明硫酸多粘菌素B益母草浸膏黄苓干膏 L-2,3-二氨基丙酸盐酸盐黄糊精EB替代品(GoldView)等均有销售.欢迎订购