Alpha-glucosidase folding during urea denaturation: Enzyme kinetics and computational prediction

Applied Biochemistry and Biotechnology

Volumn 160, Issue 5, 2010, Pages 1341-1355

  Wu, Xue Qiang ^a   Wang, Jun ^b   Lü, Zhi Rong ^a   Tang, Hong Min ^c   Park, Daeui ^d   Oh, Sang Ho ^d   Bhak, Jong ^d   Shi, Long ^a   Park, Yong Doo ^a,c   Zou, Fei ^a  

^a SOUTHERN MEDICAL UNIVERSITY   (China)

^b Shenzhen University School of Medicine   (China)

^c TSINGHUA UNIVERSITY   (China)

^d Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

Author keywords

Alpha glucosidase; Docking simulation; Urea unfolding

Indexed keywords

3D STRUCTURE; COMPUTATIONAL PREDICTIONS; DOCKING SIMULATION; DOCKING SIMULATIONS; DOSE-DEPENDENT MANNER; FIRST ORDER REACTIONS; FOLDING INTERMEDIATES; GLUCOSIDASE; HYDROPHOBIC SURFACES; STRUCTURAL CHANGE;

AGGLOMERATION; DOCKING; ENZYME KINETICS; ENZYMES; HYDROPHOBICITY; METABOLISM; SURFACE CHEMISTRY;

UREA;

ALPHA GLUCOSIDASE; DOCKING PROTEIN; UREA;

ARTICLE; COMPUTER MODEL; CONTROLLED STUDY; DENATURATION; ENZYME INACTIVATION; ENZYME KINETICS; HYDROPHOBICITY; PREDICTION; PROTEIN FOLDING; SIGNAL TRANSDUCTION;

ALPHA-GLUCOSIDASES; ANILINO NAPHTHALENESULFONATES; COMPUTATIONAL BIOLOGY; ENZYME ACTIVATION; KINETICS; MOLECULAR DYNAMICS SIMULATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; SACCHAROMYCES CEREVISIAE; SOLUTIONS; SPECTROMETRY, FLUORESCENCE; TIME FACTORS; UREA;

EID: 77949293261     PISSN: 02732289     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12010-009-8636-6     Document Type: Article

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