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

Research output: Contribution to journalArticlepeer-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 languageEnglish
Pages (from-to)556-558
JournalChemBioChem
Volume12
Issue number4
DOIs
Publication statusPublished - 7 Mar 2011

Keywords

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

Fingerprint

Dive into the research topics of 'Morphological differences between β<sub>2</sub>-microglobulin in fibrils and inclusion bodies'. Together they form a unique fingerprint.

Cite this