Distance mapping in proteins using fluorescence spectroscopy: The tryptophan-induced quenching (TrIQ) method

Biochemistry

Volumn 49, Issue 45, 2010, Pages 9722-9731

  Mansoor, Steven E ^a   Dewitt, Mark A ^a   Farrens, David L ^a  

^a OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL CHANGE; CONFORMATIONAL DYNAMICS; CYSTEINE RESIDUES; FLUORESCENCE RESONANCE ENERGY TRANSFER; MAPPING DISTANCE; PROTEIN INTERACTION; PROTEIN STRUCTURES; REAL TIME; ROTATIONAL FLEXIBILITY; SHORT DISTANCES; SPECTRAL PROPERTIES; STRUCTURAL CHANGE; T4 LYSOZYME;

AMINO ACIDS; ENERGY TRANSFER; FLUORESCENCE SPECTROSCOPY; FLUOROPHORES; PROBES; PROTEINS; SPHERES;

QUENCHING;

CYSTEINE DERIVATIVE; FLUORESCENT DYE; LYSOZYME; TRYPTOPHAN;

ARTICLE; BACTERIAL CELL; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ESCHERICHIA COLI; FLUORESCENCE RESONANCE ENERGY TRANSFER; FLUORESCENCE SPECTROSCOPY; GENE MAPPING; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN STRUCTURE; QUANTUM YIELD; THERMODYNAMICS; THERMOSTABILITY;

AMINO ACIDS; ANISOTROPY; BACTERIOPHAGE T4; FLUORESCENCE RESONANCE ENERGY TRANSFER; MODELS, MOLECULAR; MURAMIDASE; PROTEIN STRUCTURE, SECONDARY; PROTEINS; SPECTROMETRY, FLUORESCENCE; STRUCTURE-ACTIVITY RELATIONSHIP; TRYPTOPHAN;

EID: 78049441725     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100907m     Document Type: Article

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