Statistical analyses of protein sequence alignments identify structures and mechanisms in signal activation of sensor histidine kinases

Molecular Microbiology

Volumn 87, Issue 4, 2013, Pages 707-712

  Szurmant, Hendrik ^a   Hoch, James A ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN HISTIDINE KINASE;

ARTICLE; AUTOPHOSPHORYLATION; BIOSTATISTICS; CARBOXY TERMINAL SEQUENCE; DIRECT COUPLING ANALYSIS; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; GENOME; HISTIDINE ADENOSINE TRIPHOSPHATASE ADENOSINE TRIPHOSPHATE BINDING DOMAIN; HISTIDINE KINASE A DOMAIN; MOLECULAR EVOLUTION; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN MODIFICATION; PROTEIN PROTEIN INTERACTION; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; SIGNAL TRANSDUCTION; STATISTICAL ANALYSIS; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; BACTERIA; BACTERIAL PROTEINS; DATA INTERPRETATION, STATISTICAL; PROTEIN KINASES; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SIGNAL TRANSDUCTION;

EID: 84873424808     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12128     Document Type: Article

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