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Morphological Differences between β 2 ‐Microglobulin in Fibrils and Inclusion Bodies
Author(s) -
Taylor Garrick F.,
Wood Stephen P.,
Mörs Karsten,
Glaubitz Clemens,
Werner Jörn M.,
Williamson Philip T. F.
Publication year - 2011
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201000582
Subject(s) - inclusion bodies , fibril , beta 2 microglobulin , inclusion (mineral) , chemistry , biophysics , amyloid fibril , protein aggregation , crystallography , biology , biochemistry , recombinant dna , mineralogy , immunology , pathology , medicine , disease , amyloid β , gene
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.