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  Production of recombinant Conkunitzin-S1 in Escherichia coli

Bayrhuber, M., Graf, R., Ferber, M., Zweckstetter, M., Imperial, J., Garrett, J. E., et al. (2006). Production of recombinant Conkunitzin-S1 in Escherichia coli. Protein Expression and Purification, 47(2), 640-644.

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 Creators:
Bayrhuber, Monika, Author
Graf, Roland, Author
Ferber, Michael1, Author              
Zweckstetter, Markus, Author
Imperial, Julita, Author
Garrett, James E., Author
Olivera, Baldomero M., Author
Terlau, Heinrich1, Author              
Becker, Stefan, Author
Affiliations:
1Molecular and cellular neuropharmacology, Max Planck Institute of Experimental Medicine, Max Planck Society, ou_2173655              

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Free keywords: Conkunitzin-S1; Kunitz domain fold; cone snail; potassium channel PROTEINS; INTEIN; EXPRESSION; PEPTIDES; CLEAVAGE; CHANNEL; SYSTEM
 Abstract: Conkunitzin-S1 from the cone snail Conus striatus is the first member of a new neurotoxin family with a canonical Kunitz domain fold. Conk-SI is 60 amino acids long and lacks one of the three conserved disulfide bonds typically found in Kunitz domain modules. It binds specifically to voltage activated potassium channels of the Shaker family. The peptide was expressed in insoluble form in fusion with an N-terminal intein. Refolding in the presence of glutathione followed by pH shift-induced cleavage of the fusion protein resulted in a functional toxin as demonstrated by voltage-clamp measurements. (c) 2006 Elsevier Inc. All rights reserved.

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Language(s): eng - English
 Dates: 2006-06
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 292179
ISI: 000238277000038
ISI: 000238277000038
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Title: Protein Expression and Purification
  Alternative Title : Protein Expression and Purification
Source Genre: Journal
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Pages: - Volume / Issue: 47 (2) Sequence Number: - Start / End Page: 640 - 644 Identifier: ISSN: 1046-5928