Biophysical studies of the interaction between a triazole derivative and bovine serum albumin by multi-spectroscopic and molecular modeling methods

Science China Chemistry

Volumn 54, Issue 5, 2011, Pages 788-796

  Fu, Jiaxin ^a,b   Wang, Kaiwei ^a   Ge, Yushu ^b   Jiang, Fenglei ^b   Sun, Xiaohong ^c   Liu, Yang ^a   Liu, Yi ^a,b  

^a YANGTZE UNIVERSITY   (China)

^b WUHAN UNIVERSITY   (China)

^c NORTHWEST UNIVERSITY   (China)

Author keywords

binding site; bovine serum albumin; fluorescence quenching; molecular modeling; triazole

Indexed keywords

BINDING CONSTANT; BINDING DISTANCE; BINDING MODES; BIOPHYSICAL STUDIES; BOVINE SERUM ALBUMIN; BOVINE SERUM ALBUMINS; CONFORMATIONAL STUDY; ENTHALPY CHANGE; ENTROPY CHANGES; FLUORESCENCE QUENCHING; FLUORESCENCE RESONANCE ENERGY TRANSFER; HYDROGEN BONDINGS; INTERMOLECULAR FORCES; MOLECULAR MODELING STUDIES; PHYSIOLOGICAL CONDITION; SECONDARY STRUCTURES; STATIC QUENCHING; STERN-VOLMER EQUATION; SUBDOMAIN; TRIAZOLE; TRIAZOLE DERIVATIVES; TRYPTOPHAN RESIDUES; UV-VIS ABSORPTIONS; VAN DER WAALS; VAN'T HOFF EQUATION;

AMINO ACIDS; BINDING ENERGY; CHEMICAL BONDS; CIRCULAR DICHROISM SPECTROSCOPY; DICHROISM; ENERGY TRANSFER; EXPERIMENTS; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; MOLECULAR MODELING; NITROGEN COMPOUNDS; QUENCHING; VAN DER WAALS FORCES;

BODY FLUIDS;

EID: 79958214340     PISSN: 16747291     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11426-011-4260-8     Document Type: Article

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