Literature DB >> 9710243

Refolding of Escherichia coli produced membrane protein inclusion bodies immobilised by nickel chelating chromatography.

H Rogl1, K Kosemund, W Kühlbrandt, I Collinson.   

Abstract

Two distinctly different membrane proteins, which produced inclusion bodies in Escherichia coli, have been refolded to reconstitute properties appropriate to their native counterparts. The method employed utilises nickel chelating chromatography, where the solubilised inclusion bodies bind, refold and elute. Our aims were to release a large pool of membrane protein for functional, mutational and crystallisation screening studies. It is hoped that the methods described here will have a general application for other membrane proteins which have formed inclusion bodies.

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Year:  1998        PMID： 9710243     DOI： 10.1016/s0014-5793(98)00825-4

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  30 in total

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Journal:  Protein Sci       Date:  2006-09       Impact factor: 6.725

4.  Bcl-XL as a fusion protein for the high-level expression of membrane-associated proteins.

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Journal:  Protein Sci       Date:  2005-03-01       Impact factor: 6.725

5.  Misfolding of a bacterial autotransporter.

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6.  Crystal structure of plant light-harvesting complex shows the active, energy-transmitting state.

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8.  Efficient co-expression of a recombinant staphopain A and its inhibitor staphostatin A in Escherichia coli.

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9.  Refolding and simultaneous purification by three-phase partitioning of recombinant proteins from inclusion bodies.

Authors:  Smita Raghava; Bipasha Barua; Pradeep K Singh; Mili Das; Lalima Madan; Sanchari Bhattacharyya; Kanika Bajaj; B Gopal; Raghavan Varadarajan; Munishwar N Gupta
Journal:  Protein Sci       Date:  2008-09-09       Impact factor: 6.725

10.  High-yield membrane protein expression from E. coli using an engineered outer membrane protein F fusion.

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Journal:  Protein Sci       Date:  2013-02-21       Impact factor: 6.725
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