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  Expansion of the genetic code enables design of a novel "gold'' class of green fluorescent proteins

Bae, J. H., Rubini, M., Jung, G., Wiegand, G., Seifert, M. H. J., Azim, M. K., et al. (2003). Expansion of the genetic code enables design of a novel "gold'' class of green fluorescent proteins. Journal of Molecular Biology, 328(5), 1071-1081.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-6BE5-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-6BE6-2
Genre: Journal Article
Alternative Title : J. Mol. Biol.

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 Creators:
Bae, J. H.1, Author              
Rubini, M.2, Author              
Jung, G., Author
Wiegand, G.2, Author              
Seifert, M. H. J.1, Author              
Azim, M. K.1, Author              
Kim, J. S.1, Author              
Zumbusch, A.1, Author              
Holak, T. A.3, Author              
Moroder, L.4, Author              
Huber, R.2, Author              
Budisa, N.5, Author              
Affiliations:
1External Organizations, ou_persistent22              
2Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              
3Holak, Tad / NMR Spectroscopy, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565154              
4Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565160              
5Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565145              

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Free keywords: green fluorescent protein; chromophore; amino acid incorporation; tryptophan; genetic code
 Abstract: Much effort has been dedicated to the design of significantly red shifted variants of the green fluorescent protein (GFP) from Aequoria victora (av). These approaches have been based on classical engineering with the 20 canonical amino acids. We report here an expansion of these efforts by incorporation of an amino substituted variant of tryptophan into the "cyan" GFP mutant, which turned it into a "gold" variant. This variant possesses a red shift in emission unprecedented for any avFP, similar to "red" FPs, but with enhanced stability and a very low aggregation tendency. An increasing number of non-natural amino acids are available for chromophore redesign (by engineering of the genetic code) and enable new general strategies to generate novel classes of tailor-made GFP proteins. (C) 2003 Elsevier Science Ltd. All rights reserved.

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Language(s): eng - English
 Dates: 2003-05-16
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 41372
ISI: 000182767000008
 Degree: -

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Title: Journal of Molecular Biology
  Alternative Title : J. Mol. Biol.
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 328 (5) Sequence Number: - Start / End Page: 1071 - 1081 Identifier: ISSN: 0022-2836