The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, σ28

Nature Structural Biology

Volumn 4, Issue 4, 1997, Pages 285-291

  Daughdrill, Gary W ^a   Chadsey, Meggen S ^b   Karlinsey, Joyce E ^b   Hughes, Kelly T ^b   Dahlquist, Frederick W ^a  

^a UNIVERSITY OF OREGON   (United States)

^b UNIVERSITY OF WASHINGTON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN INHIBITOR; SIGMA FACTOR;

ARTICLE; CARBOXY TERMINAL SEQUENCE; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE;

BACTERIAL PROTEINS; BINDING SITES; FLAGELLA; MAGNETIC RESONANCE SPECTROSCOPY; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; SIGMA FACTOR; TIME FACTORS;

EID: 0030980926     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0497-285     Document Type: Article

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