Using an amino acid fluorescence resonance energy transfer pair to probe protein unfolding: Application to the villin headpiece subdomain and the LysM domain

Biochemistry

Volumn 47, Issue 42, 2008, Pages 11070-11076

  Glasscock, Julie M ^a   Zhu, Yongjin ^a   Chowdhury, Pramit ^a   Tang, Jia ^a   Gai, Feng ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINATION; AMINES; AMINO ACIDS; CONCENTRATION (PROCESS); DICHROISM; ENERGY TRANSFER; FLUORESCENCE; LIGHT EMISSION; LUMINESCENCE; MOLECULAR INTERACTIONS; OPTICAL PROPERTIES; ORGANIC ACIDS; PROTEINS; RESONANCE; SOLVENT EXTRACTION; THERMODYNAMICS; UREA;

CIRCULAR DICHROISMS; CONFORMATIONAL STUDIES; CONSISTENT; DENATURANT CONCENTRATIONS; DENATURED STATES; DISCRETE STEPS; EFFICIENT; FLUORESCENCE RESONANCE ENERGY TRANSFERS; FOLDING PATHWAYS; LINKING; NATURAL AMINO ACIDS; PEPTIDE SYNTHESIS; PROTEIN EXPRESSIONS; QUALITATIVE INFORMATIONS; QUANTITATIVE; RESIDUAL STRUCTURES; STRUCTURAL INFORMATIONS; SUBDOMAIN; THERMODYNAMIC PARAMETERS; VILLIN HEADPIECES;

PROTEIN FOLDING;

AMINO ACID; UREA; VILLIN;

ARTICLE; CIRCULAR DICHROISM; FLUORESCENCE RESONANCE ENERGY TRANSFER; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN STRUCTURE; THERMODYNAMICS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CIRCULAR DICHROISM; FLUORESCENCE RESONANCE ENERGY TRANSFER; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUCOPROTEINS; MUTAGENESIS, SITE-DIRECTED; NEUROFILAMENT PROTEINS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY; UREA;

EID: 54349127109     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi8012406     Document Type: Article

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