Hydrogen/deuterium exchange mass spectrometry and site-directed disulfide cross-linking suggest an important dynamic interface between the two lysostaphin domains

Antimicrobial Agents and Chemotherapy

Volumn 57, Issue 4, 2013, Pages 1872-1881

  Lu, Hai Rong ^a,c   Gu, Mei Gang ^b   Huang, Qiang ^a   Huang, Jin Jiang ^a   Lu, Wan Ying ^c   Lu, Hong ^a   Huang, Qing Shan ^a,c  

^a FUDAN UNIVERSITY   (China)

^b ROCKEFELLER UNIVERSITY   (United States)

^c Shanghai Hi Tech United Bio Technological R and D Co Ltd   (China)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; DISULFIDE; HYDROGEN; LYSOSTAPHIN; PEPTIDOGLYCAN;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CROSS LINKING; DEUTERIUM HYDROGEN EXCHANGE; DISULFIDE BOND; ENZYME SUBSTRATE COMPLEX; MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; STAPHYLOCOCCUS AUREUS; STAPHYLOCOCCUS INFECTION;

DEUTERIUM; HYDROGEN; LYSOSTAPHIN; MASS SPECTROMETRY; SODIUM CHLORIDE; STAPHYLOCOCCUS AUREUS;

EID: 84875179658     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.02348-12     Document Type: Article

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