Betts S, King J
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139, USA.
Structure. 1999 Jun 15;7(6):R131-9. doi: 10.1016/s0969-2126(99)80078-1.
The in vivo and in vitro folding, assembly and misfolding of an elongated protein, the thermostable tailspike adhesin of phage P22, reveals important aspects of the sequence control of chain folding as well as its failure mode, inclusion body formation.
噬菌体P22的热稳定尾刺粘附素这种细长蛋白质在体内和体外的折叠、组装及错误折叠,揭示了链折叠序列控制的重要方面及其失败模式——包涵体形成。