caa a22 4500 378941003 CHVBK 20180305123652.0 cr unu---uuuuu 161128e20041001xx s 000 0 eng 10.1515/BC.2004.117 doi (NATIONALLICENCE)gruyter-10.1515/BC.2004.117 Designing novel spectral classes of proteins with a tryptophan-expanded genetic code [Elektronische Daten] [Nediljko Budisa, Prajna Paramita Pal] 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. © Walter de Gruyter Biochemistry nationallicence Molecular biology nationallicence Cellular biology nationallicence analogues nationallicence engineering nationallicence fluorescence nationallicence genetic code nationallicence tryptophan nationallicence Budisa Nediljko Max-Planck-Institut für Biochemie, Am Klopferspitz 18A, D-82152 Martinsried, Germany aut Paramita Pal Prajna Max-Planck-Institut für Biochemie, Am Klopferspitz 18A, D-82152 Martinsried, Germany aut Biological Chemistry Walter de Gruyter 385/10(2004-10-01), 893-904 1431-6730 385:10<893 2004 385 bchm https://doi.org/10.1515/BC.2004.117 text/html Onlinezugriff via DOI 1 research article jats NATIONALLICENCE 856 40 https://doi.org/10.1515/BC.2004.117 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Budisa Nediljko Max-Planck-Institut für Biochemie, Am Klopferspitz 18A, D-82152 Martinsried, Germany aut NATIONALLICENCE 700 1- Paramita Pal Prajna Max-Planck-Institut für Biochemie, Am Klopferspitz 18A, D-82152 Martinsried, Germany aut NATIONALLICENCE 773 0- Biological Chemistry Walter de Gruyter 385/10(2004-10-01), 893-904 1431-6730 385:10<893 2004 385 bchm CC0 http://creativecommons.org/publicdomain/zero/1.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-gruyter