Multiple asparagine deamidation of Bacillus anthracis protective antigen causes charge isoforms whose complexity correlates with reduced biological activity

Proteins: Structure, Function and Genetics

Volumn 68, Issue 2, 2007, Pages 458-479

  Powell, Bradford S ^a   Enama, Jeffrey T ^a   Ribot, Wilson J ^a   Webster, Wendy ^a   Little, Stephen ^a   Hoover, Timothy ^a   Adamovicz, Jeffrey J ^a   Andrews, Gerard P ^a,b  

^a UNITED STATES ARMY MEDICAL RESEARCH INSTITUTE OF INFECTIOUS DISEASES   (United States)

^b UNIVERSITY OF WYOMING   (United States)

Author keywords

Anthrax toxin; Anthrax vaccine; Capillary isoelectric focusing; Computational model; Heavy isotope; Iso aspartate; Liquid chromatography ion trap tandem mass spectrometry; Protein degradation; Succinimide intermediate; Two dimensional gel electrophoresis

Indexed keywords

ANTHRAX TOXIN; ANTIGEN; ASPARAGINE; BACTERIAL ANTIGEN; PROTECTIVE ANTIGEN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS ANTHRACIS; CONTROLLED STUDY; DEAMINATION; FERMENTATION; LIQUID CHROMATOGRAPHY; NONHUMAN; PRIORITY JOURNAL; PROTEIN MODIFICATION; PROTEIN STRUCTURE; TANDEM MASS SPECTROMETRY;

AMINO ACID SEQUENCE; ANTIGENS, BACTERIAL; ASPARAGINE; ASPARTIC ACID; BACILLUS ANTHRACIS; BACTERIAL PROTEINS; MASS SPECTROMETRY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN ISOFORMS; PROTEIN PROCESSING, POST-TRANSLATIONAL; RECOMBINANT PROTEINS;

BACILLUS ANTHRACIS;

EID: 34250796766     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21432     Document Type: Article

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