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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2017: 3.022

CiteScore 2017: 2.81

SCImago Journal Rank (SJR) 2017: 1.562
Source Normalized Impact per Paper (SNIP) 2017: 0.705

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1437-4315
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Volume 385, Issue 10

Issues

Designing novel spectral classes of proteins with a tryptophan-expanded genetic code

Nediljko Budisa / Prajna Paramita Pal
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2004.117

Abstract

Fluorescence methods are now well-established and powerful tools to study biological macromolecules. The canonical amino acid tryptophan (Trp), encoded by a single UGG triplet, is the main reporter of intrinsic fluorescence properties of most natural proteins and peptides and is thus an attractive target for tailoring their spectral properties. Recent advances in research have provided substantial evidence that the natural protein translational machinery can be genetically reprogrammed to introduce a large number of non-coded (i.e. noncanonical) Trp analogues and surrogates into various proteins. Especially attractive targets for such an engineering approach are fluorescent proteins in which the chromophore is formed post-translationally from an amino acid sequence, like the green fluorescent protein from Aequorea victoria. With the currently available translationally active fluoro-, hydroxy-, amino-, halogen-, and chalcogen-containing Trp analogues and surrogates, the traditional methods for protein engineering and design can be supplemented or even fully replaced by these novel approaches. Future research will provide a further increase in the number of Trp-like amino acids that are available for redesign (by engineering of the genetic code) of native Trp residues and enable novel strategies to generate proteins with tailored spectral properties.

Keywords: analogues; engineering; fluorescence; genetic code; tryptophan

About the article

Published Online: 2005-06-01

Published in Print: 2004-10-01


Citation Information: Biological Chemistry, Volume 385, Issue 10, Pages 893–904, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2004.117.

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Inchan Kwon, Eun Sil Choi, and Nediljko Budisa
PLOS ONE, 2016, Volume 11, Number 3, Page e0152826
[2]
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[3]
Michael Georg Hoesl, Maud Larregola, Haissi Cui, and Nediljko Budisa
Journal of Peptide Science, 2010, Volume 16, Number 10, Page 589
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Sandra Lepthien, Lars Merkel, and Nediljko Budisa
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Sandra Lepthien, Lars Merkel, and Nediljko Budisa
Angewandte Chemie, 2010, Volume 122, Number 32, Page 5576
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Lars Merkel, Michael G. Hoesl, Marcel Albrecht, Andreas Schmidt, and Nediljko Budisa
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S. Lepthien, M. G. Hoesl, L. Merkel, and N. Budisa
Proceedings of the National Academy of Sciences, 2008, Volume 105, Number 42, Page 16095
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