Morphological Differences between β2-Microglobulin in Fibrils and Inclusion Bodies

Autor:	Jörn M. Werner, Philip T. F. Williamson, Steve P. Wood, Karsten Mörs, Garrick F. Taylor, Clemens Glaubitz
Rok vydání:	2011
Předmět:	Amyloid Protein Folding Magnetic Resonance Spectroscopy macromolecular substances 010402 general chemistry Fibril 01 natural sciences Biochemistry Inclusion bodies amyloid fibrils 03 medical and health sciences Humans solid-state NMR spectroscopy Molecular Biology 030304 developmental biology Inclusion Bodies 0303 health sciences Beta-2 microglobulin Chemistry Communication Organic Chemistry Amyloid fibril 0104 chemical sciences Over expression Biophysics Molecular Medicine microglobulin Protein folding beta 2-Microglobulin
Zdroj:	Chembiochem
ISSN:	1439-4227
DOI:	10.1002/cbic.201000582
Popis:	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.
Databáze:	OpenAIRE
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