摘要：The computational design of transmembrane proteins with more than one membrane-spanning region remains a major challenge. We report the design of transmembrane monomers, homodimers, trimers, and tetramers with 76 to 215 residue subunits containing two to four membrane-spanning regions and up to 860 total residues that adopt the target oligomerization state in detergent solution. The designed proteins localize to the plasma membrane in bacteria and in mammalian cells, and magnetic tweezer unfolding experiments in the membrane indicate that they are very stable. Crystal structures of the designed dimer and tetramer—a rocket-shaped structure with a wide cytoplasmic base that funnels into eight transmembrane helices—are very close to the design models. Our results pave the way for the design of multispan membrane proteins with new functions.

文献：Science 02 Mar 2018:Vol. 359, Issue 6379, pp. 1042-1046, http://science.sciencemag.org/content/359/6379/1042

简介：卢培龙博士，2009年毕业于中国科学技术大学并获得理学学士学位，2014年毕业于清华大学并获得理学博士学位。博士期间师从施一公教授，主要进行膜蛋白的结构与功能研究。自2015年一月至今，在华盛顿大学David Baker教授实验室进行博士后研究，主要研究方向是膜蛋白设计。