Thermodynamic analysis of denaturant-induced unfolding of HodC69S protein supports a three-state mechanism

Biochemistry

Volumn 47, Issue 27, 2008, Pages 7116-7126

  Boehm, Kristian ^a   Guddorf, Jessica ^a   Albers, Alexander ^a   Kamiyama, Tadashi ^b   Fetzner, Susanne ^a   Hinz, H J ^a  

^a UNIVERSITY OF MÜNSTER   (Germany)

^b KINKI UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

MECHANISMS; MOLECULAR INTERACTIONS; THERMOANALYSIS; THERMODYNAMICS;

(LIQUID + LIQUID) EQUILIBRIUM; STABILITY PARAMETERS;

THERMODYNAMIC STABILITY;

1H 3 HYDROXY 4 OXOQUINALDINE 2,4 DIOXYGENASE; CYSTEINE; DIOXYGENASE; GUANIDINE; HEXAHISTIDINE; QUINALDINE DERIVATIVE; SERINE; UREA;

AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; DISULFIDE BOND; ENZYME ACTIVITY; ENZYME STRUCTURE; FLUORESCENCE; LIGHT SCATTERING; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; THERMODYNAMICS;

ARTHROBACTER; CIRCULAR DICHROISM; DIOXYGENASES; DISULFIDES; LIGHT; MUTANT PROTEINS; OXIDATION-REDUCTION; PROTEIN DENATURATION; PROTEIN FOLDING; SCATTERING, RADIATION; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS; UREA;

EID: 46849091132     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800554v     Document Type: Article

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