Morphological differences between β(2) -microglobulin in fibrils and inclusion bodies
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 fib...
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| Veröffentlicht in: | Chembiochem : a European journal of chemical biology 2011-03, Vol.12 (4), p.556-558 |
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| container_title | Chembiochem : a European journal of chemical biology |
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| creator | Taylor, Garrick F Wood, Stephen P Mörs, Karsten Glaubitz, Clemens Werner, Jörn M Williamson, Philip T F |
| description | 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. |
| doi_str_mv | 10.1002/cbic.201000582 |
| format | Article |
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| ispartof | Chembiochem : a European journal of chemical biology, 2011-03, Vol.12 (4), p.556-558 |
| issn | 1439-7633 |
| language | eng |
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| source | MEDLINE; Access via Wiley Online Library |
| subjects | Amyloid - chemistry beta 2-Microglobulin - chemistry Humans Inclusion Bodies - chemistry Magnetic Resonance Spectroscopy Protein Folding |
| title | Morphological differences between β(2) -microglobulin in fibrils and inclusion bodies |
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