Structural perturbation of human hemoglobin on glutathionylation probed by hydrogen-deuterium exchange and MALDI mass spectrometry

Bioconjugate Chemistry

Volumn 22, Issue 4, 2011, Pages 785-793

  Mitra, Gopa ^a   Muralidharan, Monita ^a   Pinto, Jennifer ^a   Srinivasan, Krishnamachari ^a   Mandal, Amit Kumar ^a  

^a ST JOHN'S NATIONAL ACADEMY OF HEALTH SCIENCES   (India)

Author keywords

[No Author keywords available]

Indexed keywords

DEUTERIUM; HYDROGEN; MASS SPECTROMETRY; MOLECULES; PEPTIDES;

CONDITION; COOPERATIVITY; DEOXYHEMOGLOBIN; GLUTATHIONYLATION; HAEMOGLOBINS; HYDROGEN/DEUTERIUM EXCHANGE; INFORMATION CONCERNING; MATRIX-ASSISTED LASER DESORPTION IONIZATION MASS SPECTROMETRY; OXYGEN AFFINITY; STRUCTURAL PERTURBATION;

HEMOGLOBIN;

AMIDE; DEOXYHEMOGLOBIN; DEUTERIUM; GLUTATHIONE; HEMOGLOBIN; HYDROGEN; ISOTOPE;

ARTICLE; CONFORMATION; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MOLECULE; PROTEIN MODIFICATION; PROTEIN PROCESSING; STRUCTURE ANALYSIS;

EID: 79954996516     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/bc100602f     Document Type: Article

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