Labeling proteins for single-molecule FRET

Cold Spring Harbor Protocols

Volumn 7, Issue 9, 2012, Pages 1009-1012

  Joo, Chirlmin ^a   Ha, Taekjip ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; ESCHERICHIA COLI PROTEIN; FLUORESCENT DYE; HELICASE; REP PROTEIN, E COLI;

ARTICLE; CHEMICAL LABELING; COLUMN CHROMATOGRAPHY; ESCHERICHIA COLI; FLUORESCENCE RESONANCE ENERGY TRANSFER; MICROSCOPY; MOLECULE; SPECTROPHOTOMETRY; TOTAL INTERNAL REFLECTION MICROSCOPY; CHEMISTRY; ENZYMOLOGY; FLUORESCENCE; METABOLISM; METHODOLOGY; STAINING;

DNA HELICASES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FLUORESCENCE; FLUORESCENCE RESONANCE ENERGY TRANSFER; FLUORESCENT DYES; PROTEINS; STAINING AND LABELING;

EID: 84865967781     PISSN: 19403402     EISSN: 15596095     Source Type: Journal    
DOI: 10.1101/pdb.prot071035     Document Type: Article

References (4)

1. Heyduk T. 2002. Measuring protein conformational changes by FRET/LRET. Curr Opin Biotechnol 13: 292-296.
2. Rasnik I, Myong S, Cheng W, Lohman TM, Ha T. 2004. DNA-binding orientation and domain conformation of the E. coli Rep helicase monomer bound to a partial duplex junction: Single-molecule studies of fluorescently labeled enzymes. J Mol Biol 336: 395-408.
3. Schatz PJ. 1993. Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: A 13 residue-consensus peptide specifies biotinylation in Escherichia coli. Biotechnology 11: 1138-1143.
4. Selvin PR. 2000. The renaissance of fluorescence resonance energy transfer. Nat Struct Biol 7: 730-734.