The relationship between chain connectivity and domain stability in the equilibrium and kinetic folding mechanisms of dihydrofolate reductase from E.coli

Protein Engineering, Design and Selection

Volumn 19, Issue 4, 2006, Pages 175-185

  Svensson, Anna Karin E ^a,b   Zitzewitz, Jill A ^a   Matthews, C Robert ^a   Smith, Virginia F ^c  

^a UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

^b PENNSYLVANIA STATE UNIVERSITY   (United States)

^c UNITED STATES NAVAL ACADEMY   (United States)

Author keywords

Circular permutation; Equilibrium intermediate; Protein folding mechanisms; Thermal denaturation; Urea denaturation

Indexed keywords

CARBON; DEMONSTRATIONS; NITROGEN; PROTEINS; THERMODYNAMIC PROPERTIES;

ADENOSINE-BINDING DOMAIN (ABD); CIRCULAR PERMUTATION; DISCONTINUOUS LOOP DOMAIN; EQUILIBRIUM INTERMEDIATE; PROTEIN FOLDING MECHANISMS; THERMAL DENATURATION; UREA DENATURATION;

ESCHERICHIA COLI;

ADENOSINE;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DENATURATION; ENZYME ACTIVITY; EQUILIBRIUM CONSTANT; ESCHERICHIA COLI; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN STABILITY; STEADY STATE;

ESCHERICHIA COLI; HEAT; KINETICS; MODELS, MOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; TETRAHYDROFOLATE DEHYDROGENASE; THERMODYNAMICS; UREA;

ESCHERICHIA COLI;

EID: 33644901015     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzj017     Document Type: Article

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