The C-terminal portion of the fibrinogen-binding protein of Streptococcus equi subsp. equi contains extensive α-helical coiled-coil structure and contributes to thermal stability

FEMS Microbiology Letters

Volumn 206, Issue 1, 2002, Pages 81-86

  Meehan, Mary ^a   Kelly, Sharon M ^b   Price, Nicholas C ^b   Owen, Peter ^a  

^a TRINITY COLLEGE DUBLIN   (Ireland)

^b UNIVERSITY OF GLASGOW   (United Kingdom)

Author keywords

Helical coiled coil structure; Circular dichroism; Fibrinogen binding protein; Streptococcus equi subsp. equi

Indexed keywords

BACTERIAL PROTEIN; FIBRINOGEN BINDING PROTEIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; COILED BODY; CONTROLLED STUDY; MOLECULAR STABILITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN SECONDARY STRUCTURE; STREPTOCOCCUS EQUI; THERMOSTABILITY;

ANIMALS; BACTERIAL PROTEINS; CARRIER PROTEINS; CIRCULAR DICHROISM; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; STREPTOCOCCUS EQUI;

EQUIDAE; EQUUS CABALLUS; STREPTOCOCCUS; STREPTOCOCCUS EQUI SUBSP. EQUI;

EID: 0037006001     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(01)00516-X     Document Type: Article

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