Effect of Lys→Arg mutation on the thermal stability of Cu,Zn superoxide dismutase: Influence on the monomer-dimer equilibrium

Protein Engineering

Volumn 9, Issue 4, 1996, Pages 323-325

  Folcarelli, S ^a   Battistoni, A ^a   Carri M T ^a   Polticelli, F ^a   Fakoni, M ^a   Nicolini, L ^b   Stella, L ^c   Rosato, N ^a   Rotilio, G ^a   Desideri, A ^a  

^a UNIVERSITY OF ROME TOR VERGATA   (Italy)

^b ISTITUTO SUPERIORE DI SANITÀ   (Italy)

^c SAPIENZA UNIVERSITY OF ROME   (Italy)

Author keywords

Fluorescence anisotropy; Heat stability; Long range interactions; Molecular modelling; Monomer dimer equilibrium

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; DIMER; MONOMER; ARGININE; LYSINE; SUPEROXIDE DISMUTASE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANISOTROPY; ARTICLE; CONTROLLED STUDY; ENZYME KINETICS; ENZYME STABILITY; ENZYME STRUCTURE; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN STABILITY; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY; XENOPUS LAEVIS; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; COMPUTER SIMULATION; GENETICS; MUTATION;

XENOPUS LAEVIS;

ANIMALS; ARGININE; COMPUTER SIMULATION; ENZYME STABILITY; LYSINE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; SUPEROXIDE DISMUTASE; XENOPUS LAEVIS;

EID: 0029665134     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/9.4.323     Document Type: Article

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