The N-terminal sequence (5-20) of thymosin β4 binds to monomeric actin in an α-helical conformation

Biochemical and Biophysical Research Communications

Volumn 222, Issue 1, 1996, Pages 127-132

  Feinberg, J ^b   Heitz, F ^b   Benyamin, Y ^b   Roustan, C ^a  

^a Centre National de la Recherche Scientifique   (France)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; DEOXYRIBONUCLEASE I; GELSOLIN; MONOMER; THYMOSIN; TRIFLUOROETHANOL; ACTIN BINDING PROTEIN; PEPTIDE FRAGMENT; THYMOSIN BETA(4); TRYPTOPHAN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CIRCULAR DICHROISM; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; AMINO ACID SEQUENCE; ANIMAL; CHEMISTRY; DRUG EFFECT; METABOLISM; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE; RABBIT; SPECTROFLUOROMETRY; ULTRASTRUCTURE;

ACTINS; AMINO ACID SEQUENCE; ANIMALS; CIRCULAR DICHROISM; GELSOLIN; MICROFILAMENT PROTEINS; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; RABBITS; SPECTROMETRY, FLUORESCENCE; THYMOSIN; TRIFLUOROETHANOL; TRYPTOPHAN;

EID: 0029664350     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.1996.0709     Document Type: Article

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