title: Optimization of heterologous protein production in Escherichia coli.
abstract: Escherichia coli has long been the primary prokaryotic host for the synthesis of heterologous proteins. Recent advances have been made in the expression of complex proteins as soluble, functional molecules, complete with prosthetic groups, disulfide bonds, and quaternary structure. The development of alternative promoter and induction strategies has improved the options available for manipulating the expression conditions, which are frequently critical to soluble yield.
authors.affiliation: Somatogen Inc., 2545 Central Avenue, Boulder, CO 80301, USA. weickert@aol.com
authors.forename: M J
authors.initials: MJ
authors.lastname: Weickert
authors.forename: D H
authors.initials: DH
authors.lastname: Doherty
authors.forename: E A
authors.initials: EA
authors.lastname: Best
authors.forename: P O
authors.initials: PO
authors.lastname: Olins
mesh_terms: D001709:Biotechnology; D004220:Disulfides / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism*; D015870:Gene Expression; D018832:Molecular Chaperones / Q000096:biosynthesis / Q000235:genetics; D011401:Promoter Regions, Genetic; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000235:genetics*
chemical_list: D004220:Disulfides; D018832:Molecular Chaperones; D011994:Recombinant Proteins