Morphological differences between β2-microglobulin in fibrils and inclusion bodies

Garrick F. Taylor; Stephen P. Wood; Karsten Mörs; Clemens Glaubitz; Jörn M. Werner; Philip T. F. Williamson

doi:10.1002/cbic.201000582

Morphological differences between β₂-microglobulin in fibrils and inclusion bodies

Garrick F. Taylor, Stephen P. Wood, Karsten Mörs, Clemens Glaubitz, Jörn M. Werner, Philip T. F. Williamson

Institute of Life Sciences and Healthcare

Research output: Contribution to journal › Article › peer-review

Abstract

Over expression of proteins in E. coli frequently results in the production of inclusion bodies. Although β₂-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.

Original language	English
Pages (from-to)	556-558
Journal	ChemBioChem
Volume	12
Issue number	4
DOIs	https://doi.org/10.1002/cbic.201000582
Publication status	Published - 7 Mar 2011

Keywords

amyloid fibrils
inclusion bodies
microglobulin
protein folding
solid-state NMR spectroscopy

Access to Document

10.1002/cbic.201000582

Cite this

@article{2c7f6825c423428faa3952da37f49cc9,

title = "Morphological differences between β2-microglobulin in fibrils and inclusion bodies",

abstract = "Over expression of proteins in E. coli frequently results in the production of inclusion bodies. Although β2-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.",

keywords = "amyloid fibrils, inclusion bodies, microglobulin, protein folding, solid-state NMR spectroscopy",

author = "Taylor, {Garrick F.} and Wood, {Stephen P.} and Karsten M{\"o}rs and Clemens Glaubitz and Werner, {J{\"o}rn M.} and Williamson, {Philip T. F.}",

year = "2011",

month = mar,

day = "7",

doi = "10.1002/cbic.201000582",

language = "English",

volume = "12",

pages = "556--558",

journal = "ChemBioChem",

issn = "1439-4227",

publisher = "Wiley-VCH Verlag",

number = "4",

}

TY - JOUR

T1 - Morphological differences between β2-microglobulin in fibrils and inclusion bodies

AU - Taylor, Garrick F.

AU - Wood, Stephen P.

AU - Mörs, Karsten

AU - Glaubitz, Clemens

AU - Werner, Jörn M.

AU - Williamson, Philip T. F.

PY - 2011/3/7

Y1 - 2011/3/7

N2 - Over expression of proteins in E. coli frequently results in the production of inclusion bodies. Although β2-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.

AB - Over expression of proteins in E. coli frequently results in the production of inclusion bodies. Although β2-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.

KW - amyloid fibrils

KW - inclusion bodies

KW - microglobulin

KW - protein folding

KW - solid-state NMR spectroscopy

U2 - 10.1002/cbic.201000582

DO - 10.1002/cbic.201000582

M3 - Article

SN - 1439-4227

VL - 12

SP - 556

EP - 558

JO - ChemBioChem

JF - ChemBioChem

IS - 4

ER -