title: Biosynthetic substitution of tyrosine in green fluorescent protein with its surrogate fluorotyrosine in Escherichia coli.
abstract: Introduction of a fluorine moiety into green fluorescent protein offers an interesting novel spectral variant. The calculated binding energy of fluorotyrosine (F-Tyr) (-8.42 kcal/mol) for tyrosyl tRNA synthetase was moderately higher than that of tyrosine (Tyr) (-8.36 kcal/mol). This result directly correlated with the expression level of F-Tyr containing GFP (38 mg/l), which was comparably higher than that of the parent GFP expression level (34 mg/l). Finally, we generated a model structure for GFP to assess possible interaction in the chromophore of the protein structure, which plays an important role in determining the spectral and folding behaviors of the F-Tyr incorporated GFP variant.
authors: School of Biotechnology, Yeungnam University, Gyeongsan, South Korea.
authors: Niraikulam
authors: N
authors: Ayyadurai
authors: Nadarajan Saravanan
authors: NS
authors: Prabhu
authors: Kanagavel
authors: K
authors: Deepankumar
authors: Aran
authors: A
authors: Kim
authors: Sun-Gu
authors: SG
authors: Lee
authors: Hyungdon
authors: H
authors: Yun
mesh_terms: D019943:Amino Acid Substitution; D004926:Escherichia coli / Q000235:genetics; D005461:Fluorine / Q000737:chemistry*; D015870:Gene Expression; D049452:Green Fluorescent Proteins / Q000737:chemistry* / Q000235:genetics*; D014443:Tyrosine / Q000031:analogs & derivatives* / Q000737:chemistry / Q000235:genetics*
chemical_list: D049452:Green Fluorescent Proteins; D005461:Fluorine; D014443:Tyrosine