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Morphological differences between beta2-microglobulin in fibrils and inclusion bodies

Morphological differences between beta2-microglobulin in fibrils and inclusion bodies
Morphological differences between beta2-microglobulin in fibrils and inclusion bodies
Over expression of proteins in E. coli frequently results in the production of inclusion bodies. Although ?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.

amyloid fibrils, inclusion bodies, microglobulin, protein folding, solid-state nmr spectroscopy
1439-4227
556-558
Taylor, Garrick F.
3ca34f42-a4cb-4b89-b3b2-08f1e1fb1489
Wood, Stephen P.
d7187a5c-6d5a-48e1-9934-b9fb69e3f43c
Moers, Karsten
272b67eb-fad6-4c5a-ade9-adf5f47d87fd
Glaubitz, Clemens
99f5e847-e6fd-4783-bc60-054bf0e15661
Werner, Jorn M.
1b02513a-8310-4f4f-adac-dc2a466bd115
Williamson, Phillip T.F.
0b7715c6-b60e-4e95-a1b1-6afc8b9f372a
Taylor, Garrick F.
3ca34f42-a4cb-4b89-b3b2-08f1e1fb1489
Wood, Stephen P.
d7187a5c-6d5a-48e1-9934-b9fb69e3f43c
Moers, Karsten
272b67eb-fad6-4c5a-ade9-adf5f47d87fd
Glaubitz, Clemens
99f5e847-e6fd-4783-bc60-054bf0e15661
Werner, Jorn M.
1b02513a-8310-4f4f-adac-dc2a466bd115
Williamson, Phillip T.F.
0b7715c6-b60e-4e95-a1b1-6afc8b9f372a

Taylor, Garrick F., Wood, Stephen P., Moers, Karsten, Glaubitz, Clemens, Werner, Jorn M. and Williamson, Phillip T.F. (2011) Morphological differences between beta2-microglobulin in fibrils and inclusion bodies. ChemBioChem, 12 (4), 556-558. (doi:10.1002/cbic.201000582).

Record type: Article

Abstract

Over expression of proteins in E. coli frequently results in the production of inclusion bodies. Although ?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.

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More information

Published date: 26 January 2011
Keywords: amyloid fibrils, inclusion bodies, microglobulin, protein folding, solid-state nmr spectroscopy
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Identifiers

Local EPrints ID: 154965
URI: http://eprints.soton.ac.uk/id/eprint/154965
DOI: doi:10.1002/cbic.201000582
ISSN: 1439-4227
PURE UUID: 238541f6-1f4a-4e51-ba41-b19fbfa88583
ORCID for Jorn M. Werner: ORCID iD orcid.org/0000-0002-4712-1833
ORCID for Phillip T.F. Williamson: ORCID iD orcid.org/0000-0002-0231-8640

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Date deposited: 08 Feb 2011 09:15
Last modified: 14 Mar 2024 02:52

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Contributors

Author: Garrick F. Taylor
Author: Stephen P. Wood
Author: Karsten Moers
Author: Clemens Glaubitz
Author: Jorn M. Werner ORCID iD
Author: Phillip T.F. Williamson ORCID iD

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