Properties of Escherichia coli EF-Tu mutants designed for fluorescence resonance energy transfer from tRNA molecules

Protein Engineering, Design and Selection

Volumn 23, Issue 3, 2010, Pages 129-136

  Perla Kajan, Joanna ^a,d   Lin, Xin ^a,e   Cooperman, Barry S ^b   Goldman, Emanuel ^a   Jakubowski, Hieronim ^a   Knudsen, Charlotte R ^c   Mandecki, Wlodek ^a  

^a RUTGERS NEW JERSEY MEDICAL SCHOOL   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c AARHUS UNIVERSITY   (Denmark)

^d POZNA UNIVERSITY OF LIFE SCIENCES   (Poland)

^e Bioarray Solutions   (United States)

Author keywords

Elongation factor Tu; FRET; Site directed mutagenesis; Structure function; Transfer RNA

Indexed keywords

AMINOACYL; C TERMINUS; ELONGATION FACTOR TU; FLUORESCENCE RESONANCE ENERGY TRANSFER; FLUORESCENCE RESONANCE ENERGY TRANSFER ASSAYS; FRET; GEL RETARDATION; GLUTATHIONE-S-TRANSFERASE; IN-VITRO; N-TERMINALS; POTENTIAL UTILITY; PROTECTION ASSAY; SINGLE CYSTEINE RESIDUE; SITE DIRECTED MUTAGENESIS; TERNARY COMPLEX;

AMINO ACIDS; ASSAYS; BINDING ENERGY; COMPLEXATION; ELONGATION; ENERGY TRANSFER; ESCHERICHIA COLI; MUTAGENESIS; RESONANCE; RNA; SYSTEM THEORY;

FLUORESCENCE;

AMINO ACID; CYSTEINE; ELONGATION FACTOR TU; GLUTATHIONE TRANSFERASE; GUANOSINE DIPHOSPHATE; POLYURIDYLIC ACID; TERNARY COMPLEX FACTOR; TRANSFER RNA;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ESCHERICHIA COLI; FLUORESCENCE RESONANCE ENERGY TRANSFER; GENE FUSION; GENE INTERACTION; IN VITRO STUDY; LABELING INDEX; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN ISOLATION;

BINDING SITES; ELECTROPHORETIC MOBILITY SHIFT ASSAY; ESCHERICHIA COLI; FACTOR XA; FLUORESCENCE RESONANCE ENERGY TRANSFER; GUANOSINE DIPHOSPHATE; HYDROLYSIS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; MUTATION; NUCLEIC ACID CONFORMATION; PEPTIDE ELONGATION FACTOR TU; PEPTIDES; PROTEIN CONFORMATION; PROTEIN ENGINEERING; RNA, TRANSFER; SEQUENCE ANALYSIS, DNA; STAINING AND LABELING;

ESCHERICHIA COLI;

EID: 76949090396     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzp079     Document Type: Article

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