Elucidating Quantitative Stability/Flexibility Relationships Within Thioredoxin and its Fragments Using a Distance Constraint Model

Journal of Molecular Biology

Volumn 358, Issue 3, 2006, Pages 882-904

  Jacobs, Donald J ^a   Livesay, Dennis R ^b   Hules, Jeremy ^c   Tasayco, Maria Luisa ^d  

^a UNIVERSITY OF NORTH CAROLINA AT CHARLOTTE   (United States)

^b CALIFORNIA STATE POLYTECHNIC UNIVERSITY   (United States)

^c CALIFORNIA STATE UNIVERSITY   (United States)

^d CITY COLLEGE OF NEW YORK   (United States)

Author keywords

folding pathways; intermediate states; kinetic trap; molecular cooperativity; thioredoxin

Indexed keywords

THIOREDOXIN;

ARTICLE; CORRELATION ANALYSIS; ESCHERICHIA COLI; HYDROGEN BOND; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; QUANTITATIVE ANALYSIS; STRUCTURAL PROTEOMICS; STRUCTURE ANALYSIS; TEMPERATURE DEPENDENCE; THEORETICAL MODEL; THERMODYNAMICS; THERMOSTABILITY;

ESCHERICHIA COLI;

EID: 33646033429     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.02.015     Document Type: Article

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