The solution structure of a monomeric, reduced form of human copper,zinc superoxide dismutase bearing the same charge as the native protein

Journal of Biological Inorganic Chemistry

Volumn 4, Issue 6, 1999, Pages 795-803

  Banci, Lucia ^a   Bertini, Ivano ^a   Del Conte, Rebecca ^a   Fadin, Roberto ^a   Mangani, Stefano ^b   Viezzoli, Maria Silvia ^a  

^a UNIVERSITY OF FLORENCE   (Italy)

^b UNIVERSITY OF SIENA   (Italy)

Author keywords

Monomeric mutants; NMR; Solution structure; Structure function relationship; Superoxide dismutase

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; DIMER; ISOENZYME; MONOMER; MUTANT PROTEIN;

ARTICLE; CONTROLLED STUDY; DISSOLUTION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME STRUCTURE; ENZYME SUBUNIT; HUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; REDUCTION; SURFACE CHARGE;

BINDING SITES; CATALYSIS; COPPER; ELECTROSTATICS; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; SUPEROXIDE DISMUTASE; ZINC;

EID: 0032714364     PISSN: 09498257     EISSN: None     Source Type: Journal    
DOI: 10.1007/s007750050353     Document Type: Article

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