title: Morphological differences between β(2) -microglobulin in fibrils and inclusion bodies.
abstract: Over expression of proteins in E. coli frequently results in the production of inclusion bodies. Although β(2) -microglobulin frequently forms fibrillar structures, our studies reveal significant differences between the protein in fibrils and inclusion bodies. This suggests that the formation of fibrils in inclusion bodies is dependent on the propensity of the protein to form fibrillar structures.
authors.affiliation: School of Biological Sciences, University of Southampton, Highfield Campus, Southampton, SO17 1BJ, UK.
authors.forename: Garrick F
authors.initials: GF
authors.lastname: Taylor
authors.forename: Stephen P
authors.initials: SP
authors.lastname: Wood
authors.forename: Karsten
authors.initials: K
authors.lastname: Mörs
authors.forename: Clemens
authors.initials: C
authors.lastname: Glaubitz
authors.forename: Jörn M
authors.initials: JM
authors.lastname: Werner
authors.forename: Philip T F
authors.initials: PT
authors.lastname: Williamson
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D006801:Humans; D002479:Inclusion Bodies / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D017510:Protein Folding; D001613:beta 2-Microglobulin / Q000737:chemistry*
chemical_list: D000682:Amyloid; D001613:beta 2-Microglobulin