Shape evolution and thermal stability of lysozyme crystals: Effect of pH and temperature

Bioprocess and Biosystems Engineering

Volumn 36, Issue 1, 2013, Pages 91-99

  Liang, Miao ^a   Jin, Fengmin ^a   Liu, Rui ^a   Yu, Yanjun ^a   Su, Rongxin ^a   Wang, Libing ^a   Qi, Wei ^a   He, Zhimin ^a  

^a TIANJIN UNIVERSITY   (China)

Author keywords

Lysozyme; Protein crystallization; Shape control; Shape evolution; Thermal stability

Indexed keywords

CRYSTAL NUCLEATION; CRYSTAL SHAPES; CRYSTALLINE PROTEIN; EFFECT OF PH; HEN EGG WHITE LYSOZYME; INFLUENCE OF PH; LYSOZYME CRYSTALS; NUCLEATION PROCESS; PH VALUE; PROTEIN CRYSTAL; PROTEIN CRYSTALLIZATION; PROTEIN MOLECULES; SHAPE CONTROL; SHAPE EVOLUTION; SHAPE-CONTROLLED; SIMPLE METHOD; THERMAL BEHAVIORS;

ASPECT RATIO; DIFFERENTIAL SCANNING CALORIMETRY; ENZYMES; NUCLEATION; PROTEINS; THERMODYNAMIC STABILITY; VAPORS;

PH EFFECTS;

LYSOZYME;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIFFERENTIAL SCANNING CALORIMETRY; MOLECULAR EVOLUTION; MOLECULAR INTERACTION; PH; PRIORITY JOURNAL; PROTEIN CROSS LINKING; STATIC ELECTRICITY; TEMPERATURE MEASUREMENT; TEMPERATURE SENSITIVITY; THERMAL ANALYSIS; THERMAL DIFFUSION; THERMOSTABILITY;

CRYSTALLIZATION; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; MATERIALS TESTING; MOLECULAR CONFORMATION; MURAMIDASE; PROTEIN CONFORMATION; TEMPERATURE;

EID: 84872346022     PISSN: 16157591     EISSN: 16157605     Source Type: Journal    
DOI: 10.1007/s00449-012-0764-7     Document Type: Article

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