Structural and functional roles of a conserved proline residue in the α2 helix of Escherichia coli thioredoxin

Protein Engineering

Volumn 10, Issue 12, 1997, Pages 1425-1432

  De Lamotte Guéry, Frédéric ^a,e   Pruvost, Christian ^b   Minard, Philippe ^c   Delsuc, Marc André ^b   Miginiac Maslow, Myroslawa ^a   Schmitter, Jean Marie ^d   Stein, Mariana ^a   Decottignies, Paulette ^a  

^a INSTITUTE OF PLANT SCIENCES PARIS SACLAY IPS2   (France)

^b CENTRE DE BIOCHIMIE STRUCTURALE   (France)

^c UNIVERSITÉ PARIS SACLAY   (France)

^d LABORATOIRE DE BIOCHIMIE   (France)

^e CEMAGREF   (France)

Author keywords

helix; NADP malate dehydrogenase activation; Protein stability; Site directed mutagenesis; Thioredoxin

Indexed keywords

ALANINE; BACTERIAL PROTEIN; MALATE DEHYDROGENASE (NADP); MUTANT PROTEIN; PROLINE; THIOREDOXIN;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; CHROMATOGRAPHY; CONTROLLED STUDY; ENZYME ACTIVATION; ESCHERICHIA COLI; FLUORESCENCE; HYDROPHOBICITY; LIGHT; MOLECULAR DYNAMICS; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN STABILITY; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; BINDING SITES; CHEMISTRY, PHYSICAL; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CONSERVED SEQUENCE; ENZYME ACTIVATION; ESCHERICHIA COLI; MALATE DEHYDROGENASE; MASS SPECTROMETRY; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NADP; OXIDATION-REDUCTION; PROLINE; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS; THIOREDOXIN;

EID: 0031414082     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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