Hydration change during the aging of phosphorylated human butyrylcholinesterase: Importance of residues aspartate-70 and glutamate-197 in the water network as probed by hydrostatic and osmotic pressures

Biochemical Journal

Volumn 343, Issue 2, 1999, Pages 361-369

  Masson, Patrick ^a   Cléry, Cécile ^a   Guerra, Patrice ^a   Redslob, Arnaud ^a   Albaret, Christine ^b   Fortier, Pierre Louis ^b  

^a CENTRE DE RECHERCHES   (France)

^b CENTRE D ETUDES DU BOUCHET   (France)

Author keywords

Hydrostatic pressure; Molecular dynamics; Osmotic pressure; Phosphorylation

Indexed keywords

ASPARTIC ACID; CHOLINESTERASE; DYFLOS; GLUTAMIC ACID; MUTANT PROTEIN; PHOSPHOPROTEIN; SOMAN; WATER;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DEALKYLATION; DIFFERENTIAL SCANNING CALORIMETRY; ELECTROPHORESIS; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME INHIBITION; ENZYME METABOLISM; ENZYME PHOSPHORYLATION; HUMAN; HYDRATION; HYDROSTATIC PRESSURE; MOLECULAR DYNAMICS; NONHUMAN; OSMOTIC PRESSURE; PH; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

ALKYLATION; AMINO ACID SUBSTITUTION; ASPARTIC ACID; BINDING SITES; BUTYRYLCHOLINESTERASE; COMPUTER SIMULATION; ENZYME STABILITY; GLUTAMIC ACID; HUMANS; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; HYDROSTATIC PRESSURE; KINETICS; MODELS, MOLECULAR; OSMOLAR CONCENTRATION; PHOSPHORYLATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, QUATERNARY; RECOMBINANT PROTEINS; SOMAN; THERMODYNAMICS; WATER;

ANIMALIA;

EID: 2442769298     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3430361     Document Type: Article

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