Mapping residual structure in intrinsically disordered proteins at residue resolution using millisecond hydrogen/deuterium exchange and residue averaging

Journal of the American Society for Mass Spectrometry

Volumn 26, Issue 4, 2015, Pages 547-554

  Keppel, Theodore R ^a,b   Weis, David D ^a  

^a UNIVERSITY OF KANSAS   (United States)

^b NONE   (United States)

Author keywords

H D exchange mass spectrometry; Intrinsically disordered protein; Residual structure

Indexed keywords

FACSIMILE; HYDROGEN; MASS SPECTROMETRY; PEPTIDES; SPECTROMETRY;

DISORDERED PROTEINS; H/D EXCHANGE; HYDROGEN/DEUTERIUM EXCHANGE; INTRINSICALLY DISORDERED PROTEINS; RESIDUAL STRUCTURE; SECONDARY STRUCTURE ELEMENTS; SINGLE RESIDUE; SPATIAL RESOLUTION;

PROTEINS;

E1A ASSOCIATED P300 PROTEIN; INTRINSICALLY DISORDERED PROTEIN; PROTEIN P160;

ARTICLE; ARTIFACT; COLLISIONALLY ACTIVATED DISSOCIATION; CONTROLLED STUDY; DEUTERIUM HYDROGEN EXCHANGE; HUMAN; LIQUID CHROMATOGRAPHY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE MAPPING; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; TANDEM MASS SPECTROMETRY; TIME OF FLIGHT MASS SPECTROMETRY; CHEMISTRY; MASS SPECTROMETRY; PROCEDURES;

DEUTERIUM EXCHANGE MEASUREMENT; INTRINSICALLY DISORDERED PROTEINS; MASS SPECTROMETRY; PEPTIDE MAPPING; PROTEIN STRUCTURE, SECONDARY;

EID: 84924859480     PISSN: 10440305     EISSN: 18791123     Source Type: Journal    
DOI: 10.1007/s13361-014-1033-6     Document Type: Article

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