Binding thermodynamics of phosphorylated inhibitors to triosephosphate isomerase and the contribution of electrostatic interactions

Journal of Molecular Biology

Volumn 405, Issue 1, 2011, Pages 158-172

  Serratos, Iris N ^a   Pérez Hernández, Gerardo ^b   Garza Ramos, Georgina ^c   Hernández Arana, Andrés ^a   González Mondragón, Edith ^a   Zubillaga, Rafael A ^a  

^a DEPARTAMENTO DE QUÍMICA   (Mexico)

^b DEPARTAMENTO DE PROCESOS Y TECNOLOGÍA   (Mexico)

^c UNIVERSIDAD NACIONAL AUTÓNOMA DE MÉXICO   (Mexico)

Author keywords

binding thermodynamics; enzymeinhibitor binding; ionic strength; multithermal titration calorimetry; structural energetics

Indexed keywords

2 PHOSPHOGLYCOLATE; ENZYME INHIBITOR; PHOSPHOGLYCOLOHYDROXAMATE; SODIUM CHLORIDE; TRIOSEPHOSPHATE ISOMERASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CIRCULAR DICHROISM; CONCENTRATION PROCESS; CONTROLLED STUDY; ENZYME BINDING; ENZYME INHIBITOR INTERACTION; FLUOROMETRY; HYDROGEN BOND; IONIC STRENGTH; ISOTHERMAL TITRATION CALORIMETRY; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN STABILITY; PROTON TRANSPORT; STATIC ELECTRICITY; SURFACE PROPERTY; THERMODYNAMICS;

EID: 78650413784     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.10.018     Document Type: Article

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