Accessibility of introduced cysteines in chemoreceptor transmembrane helices reveals boundaries interior to bracketing charged residues

Protein Science

Volumn 13, Issue 6, 2004, Pages 1466-1475

  Boldog, Thomas ^a   Hazelbauer, Gerald L ^a  

^a University of Missouri   (United States)

Author keywords

Bacterial chemoreceptors; Cysteine scanning; Hydrophobic hydrophilic boundaries; Lipid bilayers; Transmembrane proteins

Indexed keywords

CYSTEINE; HYDROCARBON; THIOL DERIVATIVE;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; CHEMORECEPTOR; ESCHERICHIA COLI; HYDROPHILICITY; HYDROPHOBICITY; LIPID BILAYER; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; CELL MEMBRANE; CROSS-LINKING REAGENTS; CYSTEINE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDROPHOBICITY; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SULFHYDRYL COMPOUNDS; X-RAY DIFFRACTION;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 2442720144     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.04648604     Document Type: Article

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