The role of the local environment of engineered Tyr to Trp substitutions for probing the denaturation mechanism of FIS

Protein Science

Volumn 20, Issue 2, 2011, Pages 302-312

  Muñiz, Virginia A ^a   Srinivasan, Saipraveen ^a   Boswell, Sarah A ^a   Meinhold, Derrick W ^a   Childs, Tawanna ^a   Osuna, Robert ^b   Colón, Wilfredo ^a  

^a RENSSELAER POLYTECHNIC INSTITUTE   (United States)

^b STATE UNIVERSITY OF NEW YORK   (United States)

Author keywords

Dimer; FIS; Fluorescence; Intermediates; Protein folding

Indexed keywords

FACTOR FOR INVERSION STIMULATION; HOMODIMER; TRYPTOPHAN; TYROSINE;

AMINO ACID SUBSTITUTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONCENTRATION RESPONSE; CONFORMATIONAL TRANSITION; ESCHERICHIA COLI; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STABILITY;

AMINO ACID SUBSTITUTION; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI PROTEINS; FACTOR FOR INVERSION STIMULATION PROTEIN; MICROSCOPY, FLUORESCENCE; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN STABILITY; TRYPTOPHAN; TYROSINE;

EID: 79251539857     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.561     Document Type: Article

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