Premium
Unnatural Amino Acid Mutagenesis of Fluorescent Proteins
Author(s) -
Wang Feng,
Niu Wei,
Guo Jiantao,
Schultz Peter G.
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201204668
Subject(s) - green fluorescent protein , fluorescence , mutagenesis , mutant , tyrosine , amino acid , chemistry , fluorescent protein , biochemistry , combinatorial chemistry , gene , physics , quantum mechanics
Tyrosine 66 of a green fluorescent protein (GFP) was substituted with unnatural amino acids carrying boronate, azido, nitro, and keto substituents. In general, the ${{\lambda _{{\rm{{\rm em}}}}^{{\rm{{\rm max}}}} }}$ values of these GFP mutants is blue‐shifted relative to that of GFP, and the fluorescence intensity of the boronate variant increases upon oxidation (see scheme). The X‐ray crystal structures of the keto and boronate GFP mutants provide explanations of their altered fluorescence properties.