Detection of early unfolding events in a dimeric protein by amide proton exchange and native electrospray mass spectrometry

Protein Science

Volumn 18, Issue 8, 2009, Pages 1620-1627

  Mobley, James A ^a   Poliakov, Anton ^a  

^a UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

Author keywords

Amide proton exchange; B. subtilis; H D exchange; Isotopic labeling; Mass spectrometry; NAD+ synthetase; Native mass spectrometry; Unfolding

Indexed keywords

AMIDE; DEUTERIUM; DIMER; HYDROGEN; ISOTOPE; NICOTINAMIDE ADENINE DINUCLEOTIDE; OLIGOMER; PROTON; SYNTHETASE;

AMIDE PROTON EXCHANGE; ARTICLE; BACILLUS SUBTILIS; CONFORMATIONAL TRANSITION; DEUTERIUM HYDROGEN EXCHANGE; DIMERIZATION; DISSOCIATION; ELECTROSPRAY MASS SPECTROMETRY; ION EXCHANGE; ISOTOPE LABELING; LIFE CYCLE; LIQUID CHROMATOGRAPHY; MELTING POINT; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN QUATERNARY STRUCTURE; THERMAL EXPOSURE;

AMIDE SYNTHASES; BACILLUS SUBTILIS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTONS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;

BACILLUS SUBTILIS;

EID: 67749108049     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.176     Document Type: Article

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