Membrane protein solubilization and structure determination using de novo–designed proteins
原文开头
Ljubica Mihaljević†, David E. Kim†, Pooja D. Bandawane†, et al. INTRODUCTION: Membrane proteins play central roles in signaling, infection, and drug responses, yet they remain among the most difficult proteins to produce and study because their water- repelling surfaces destabilize them outside of the membrane. Given that these proteins are embedded within lipid membranes, their extraction relies on detergents. This is a laborious, multistep process that requires extensive optimization and often compromises protein stability and complicates downstream analysis. For example, outer membrane proteins of the Gram- negative bacteria Treponema pallidum, which causes syphilis, are promising vaccine candidates. However, they are difficult to express in Escherichia coli, and their solubilization without detergents could facilitate monoclonal antibody discovery and vaccine design. …
摘自《科学》(Science)第393卷 第6806期 · 2026年7月2日。仅引用开头一小段供了解文章,版权归原刊所有,全文请阅读原刊。