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The use of unnatural amino acids to study and engineer protein function.
Neumann-Staubitz, Petra; Neumann, Heinz.
Afiliación
  • Neumann-Staubitz P; Georg August University Göttingen, GZMB, Applied Synthetic Biology Group, Justus-von-Liebig Weg 11, 37077 Göttingen, Germany.
  • Neumann H; Georg August University Göttingen, GZMB, Applied Synthetic Biology Group, Justus-von-Liebig Weg 11, 37077 Göttingen, Germany; Max-Planck-Institute for Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany. Electronic address: heinz.neumann@mpi-dortmund.mpg.de.
Curr Opin Struct Biol ; 38: 119-28, 2016 06.
Article en En | MEDLINE | ID: mdl-27318816
The expansion of the genetic code for the incorporation of unnatural amino acids (UAAs) in proteins of bacteria, yeasts, mammalian cells or whole animals provides molecular and structural biologists with an amazing kit of novel tools. UAAs can be used to investigate the structure and dynamics of proteins, to study their interactions or to control their activity in living cells. Incorporation of UAAs with bioorthogonal reactivity facilitates the site-specific installation of labels for spectroscopy and microscopy. Light-activatable crosslinker UAAs can be used to trap interacting molecules in living cells with a precision almost at the structural level. Post-translational modifications such as lysine acetylation and serine phosphorylation can be directly encoded to analyse their impact on protein function, and caging groups can be installed on critical residues to create light-activatable proteins. In this review we highlight recent applications of this technology to investigate protein function.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ingeniería de Proteínas / Proteínas / Aminoácidos Límite: Animals Idioma: En Revista: Curr Opin Struct Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2016 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ingeniería de Proteínas / Proteínas / Aminoácidos Límite: Animals Idioma: En Revista: Curr Opin Struct Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2016 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido