Protein in Peak 11 Channel Lipoprotein

The existence of this peak was reported in 1969 by Inouye and Guthrie. However, this peak was identified only recently as the free form of a structural lipoprotein, which has been reported by Braun and his coworkers to bind covalently to the peptidoglycan. This lipoprotein is the most abundant protein in E. coli and an excellent membrane protein to investigate because of its many interesting characteristics. Indeed, this lipoprotein is one of the best studied membrane proteins. 

Recently a three-dimensional molecular model of the arrangement of this protein has been proposed which suggests that complexes of the lipoprotein form passive diffusion channels in the outer membrane. Our extensive work on the chemical properties, in vivo and in vitro biosynthesis, assembly, and paracrystallization of the protein will be discussed in a separate section of this chapter. 

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