Alteration of the quaternary structure of glutamate dehydrogenase from Clostridium symbiosum by a single mutation distant from the subunit interfaces

European Biophysics Journal

Volumn 25, Issue 5-6, 1997, Pages 417-422

  Dean, Jonathan L E ^a   Cölfen, Helmut ^b,d   Harding, Stephen E ^b   Rice, David W ^a   Engel, Paul C ^c  

^a UNIVERSITY OF SHEFFIELD   (United Kingdom)

^b UNIVERSITY OF NOTTINGHAM   (United Kingdom)

^c UNIVERSITY COLLEGE DUBLIN   (Ireland)

^d MAX PLANCK INSTITUTE OF COLLOIDS AND INTERFACES   (Germany)

Author keywords

Allostery; Analytical ultracentrifugation; Glutamate dehydrogenase; Quaternary structure; Subunit communication

Indexed keywords

ARTICLE; CLOSTRIDIUM; ENZYME ACTIVE SITE; ENZYME REGULATION; ENZYME STRUCTURE; GEL FILTRATION; MOLECULAR WEIGHT; PROTEIN QUATERNARY STRUCTURE; SEDIMENTATION RATE; STOICHIOMETRY; X RAY CRYSTALLOGRAPHY;

CHROMATOGRAPHY, GEL; CLONING, MOLECULAR; CLOSTRIDIUM; CRYSTALLOGRAPHY, X-RAY; DITHIONITROBENZOIC ACID; ESCHERICHIA COLI; GLUTAMATE DEHYDROGENASE; MACROMOLECULAR SUBSTANCES; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; ULTRACENTRIFUGATION;

CLOSTRIDIUM; CLOSTRIDIUM SYMBIOSUM;

EID: 18844482528     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002490050055     Document Type: Article

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