Coupling of folding and binding of thymosin β4 upon interaction with monomeric actin monitored by nuclear magnetic resonance

Journal of Biological Chemistry

Volumn 279, Issue 22, 2004, Pages 23637-23645

  Domanski, Michael ^a   Hertzog, Maud ^a   Coutant, Jérôme ^a   Gutsche Perelroizen, Irina ^a   Bontems, François ^a   Carlier, Marie France ^a   Guittet, Eric ^a   Van Heijenoort, Carine ^a  

^a CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; CHEMICAL BONDS; CROSSLINKING; MONOMERS; NITROGEN; PROTEINS;

BIOLOGICAL FUNCTIONS; MONOMERIC ACTIN;

NUCLEAR MAGNETIC RESONANCE;

ACTIN; MONOMER; SUBTILISIN; THYMOSIN BETA4;

ACTIN FILAMENT; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; COUPLING FACTOR; CROSS LINKING; DNA FLANKING REGION; DRUG RECEPTOR BINDING; MONITORING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE;

ACTINS; ANIMALS; BINDING SITES; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN FOLDING; THYMOSIN;

ANIMALIA;

EID: 2542492280     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M311413200     Document Type: Article

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