Refolding of lysozyme by quasistatic and direct dilution reaction paths: A first-order-like state transition

Physical Review E - Statistical Physics, Plasmas, Fluids, and Related Interdisciplinary Topics

Volumn 70, Issue 1, 2004, Pages 8-

  Chang, Chia Ching ^a   Yeh, Xu Cheng ^a,b   Lee, Hui Ting ^a   Lin, Po Yen ^a,b   Kan, Lou Sing ^b  

^a NATIONAL DONG HWA UNIVERSITY   (Taiwan)

^b INSTITUTE OF CHEMISTRY   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

BONDING; DIALYSIS; DIFFERENTIAL SCANNING CALORIMETRY; DNA; LIGHT SCATTERING; MATHEMATICAL MODELS; MELTING; MOLECULAR WEIGHT; OXIDATION; PARTICLE SIZE ANALYSIS; RAMAN SCATTERING; SPECTROSCOPIC ANALYSIS; THERMODYNAMIC STABILITY;

DYNAMIC LIGHT SCATTERING; MOLECULAR WEIGHT CUTOFF (MWCO); SEMIPERMEABLE MEMBRANE DEVICES; THERMAL EQUILIBRIUM DIALYSIS (TED);

ENZYMES;

HEN EGG LYSOZYME; LYSOZYME; UREA;

ARTICLE; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; EVALUATION; KINETICS; PH; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SOLUBILITY; TEMPERATURE; VALIDATION STUDY;

HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, CHEMICAL; MODELS, MOLECULAR; MURAMIDASE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SOLUBILITY; TEMPERATURE; UREA;

EID: 42749100762     PISSN: 1063651X     EISSN: None     Source Type: Journal    
DOI: 10.1103/PhysRevE.70.011904     Document Type: Article

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