Role of electrostatic interactions on the affinity of thioredoxin for target proteins: Recognition of chloroplast fructose-1,6-bisphosphatase by mutant Escherichia coli thioredoxins

Journal of Biological Chemistry

Volumn 273, Issue 26, 1998, Pages 16273-16280

  Mora Garcia, S ^a   Rodriguez Suarez, R ^a   Wolosiuk, R A ^a  

^a FUNDACIÓN INSTITUTO LELOIR   (Argentina)

Author keywords

[No Author keywords available]

Indexed keywords

DISULFIDE; FRUCTOSE BISPHOSPHATASE; THIOREDOXIN;

AMINO ACID SUBSTITUTION; ARTICLE; BACTERIUM MUTANT; CHLOROPLAST; ESCHERICHIA COLI; MOLECULAR CLONING; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN TARGETING;

BRASSICA; CHLOROPLASTS; ELECTROSTATICS; ESCHERICHIA COLI; FRUCTOSE-BISPHOSPHATASE; KINETICS; LYSINE; MUTAGENESIS, SITE-DIRECTED; PLANT PROTEINS; PROTEIN DISULFIDE REDUCTASE (GLUTATHIONE); STRUCTURE-ACTIVITY RELATIONSHIP; THIOREDOXIN;

EID: 0032568925     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.26.16273     Document Type: Article

References (61)