AHSP (α-haemoglobin-stabilizing protein) stabilizes apo-α-haemoglobin in a partially folded state

Biochemical Journal

Volumn 432, Issue 2, 2010, Pages 275-282

  Krishna Kumar, Kaavya ^a   Dickson, Claire F ^b   Weiss, Mitchell J ^c   Mackay, Joel P ^a   Gell, David A ^b  

^a UNIVERSITY OF SYDNEY   (Australia)

^b UNIVERSITY OF TASMANIA   (Australia)

^c UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

haemoglobin stabilizing protein (AHSP); Aggregation; Apo haemoglobin; Chaperone

Indexed keywords

AGGREGATION; BINDING EVENTS; CHAPERONE; FOLDED STATE; HAEM IRON; HAEMOGLOBINS; HETERODIMERIC COMPLEXES; NMR SPECTROSCOPY; REDOX ACTIVITY; SELF-ASSOCIATIONS;

HEMOGLOBIN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; REDOX REACTIONS;

ASSOCIATION REACTIONS;

ALPHA HEMOGLOBIN STABILIZING PROTEIN; CHAPERONE; HEME; HEMOGLOBIN; IRON BINDING PROTEIN; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; COMPLEX FORMATION; DIMERIZATION; IRON BINDING CAPACITY; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; THERMOSTABILITY;

APOPROTEINS; BLOOD PROTEINS; CIRCULAR DICHROISM; DIMERIZATION; DRUG STABILITY; HEMOGLOBIN A; HEMOGLOBINS; HUMANS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; PEPTIDE FRAGMENTS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; SCATTERING, RADIATION; SOLUBILITY; THERMODYNAMICS;

EID: 78649597558     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20100642     Document Type: Article

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