Use of different proteases working in acidic conditions to improve sequence coverage and resolution in hydrogen/deuterium exchange of large proteins

Rapid Communications in Mass Spectrometry

Volumn 17, Issue 21, 2003, Pages 2387-2393

  Cravello, Laetitia ^a   Lascoux, David ^a   Forest, Eric ^a  

^a INSTITUT DE BIOLOGIE STRUCTURALE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

DEUTERIUM; HYDROGEN; IMAGE RESOLUTION; PEPTIDES; PROTEOLYSIS; TEMPERATURE;

ACIDIC CONDITIONS; HYDROGEN EXCHANGE; HYDROGEN/DEUTERIUM EXCHANGE; LOWS-TEMPERATURES; PROTEIN DYNAMICS; PROTEINS STRUCTURES; SEQUENCE COVERAGES; SPATIAL RESOLUTION; STRUCTURAL BIOLOGY; STRUCTURE DYNAMICS;

MASS SPECTROMETRY;

DEUTERIUM; FUNGAL ENZYME; HYDROGEN; PENICILLIN BINDING PROTEIN; PENICILLIN BINDING PROTEIN X; PEPSIN A; PEPTIDE; PROTEASE XIII; PROTEASE XVIII; PROTEINASE; UNCLASSIFIED DRUG;

ACCURACY; ACIDITY; AMINO ACID SEQUENCE; ARTICLE; ASPERGILLUS; ASPERGILLUS SAITOI; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SPECIFICITY; HYDROGEN EXCHANGE; LOW TEMPERATURE PROCEDURES; MASS SPECTROMETRY; MOLECULAR DYNAMICS; MOLECULAR MODEL; MOLECULAR SIZE; NONHUMAN; PEPTIDE MAPPING; PH; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTON TRANSPORT; REPRODUCIBILITY; RHIZOPUS; TECHNIQUE; X RAY CRYSTALLOGRAPHY;

EID: 0242386421     PISSN: 09514198     EISSN: None     Source Type: Journal    
DOI: 10.1002/rcm.1207     Document Type: Article

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