Comparison of continuous and pulsed labeling amide hydrogen exchange/mass spectrometry for studies of protein dynamics

Journal of the American Society for Mass Spectrometry

Volumn 10, Issue 8, 1999, Pages 675-684

  Deng, Y ^a   Zhang, Z ^a   Smith, D L ^a  

^a UNIVERSITY OF NEBRASKA LINCOLN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FRUCTOSE BISPHOSPHATE ALDOLASE;

PROTEIN;

ARTICLE; DYNAMICS; ION EXCHANGE; KINETICS; MASS; MASS SPECTROMETRY; PROTEIN BINDING; PROTEIN FOLDING; TEMPERATURE; THERMODYNAMICS; X RAY DIFFRACTION;

AMIDES; HYDROGEN; MASS SPECTROMETRY; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEINS;

EID: 0033473768     PISSN: 10440305     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1044-0305(99)00038-0     Document Type: Article

References (30)

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20. The crystal structure of human muscle aldolase at 3.0 A resolution
21. Molecular architecture of rabbit skeletal muscle aldolase at 2.7-A resolution
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