Human serum albumin (HSA) participates in heme scavenging, the bound heme turning out to be a reactivity center and a powerful spectroscopic probe. Here, the reversible unfolding of heme-HSA has been investigated by H-1-NMR relaxometry, circular dichroism, and absorption spectroscopy. In the presence of 6 equiv of myristate ( thus fully saturating all available fatty acid binding sites in serum heme-albumin), 1.0 M guanidinium chloride induces some unfolding of heme-HSA, leading to the formation of a folding intermediate; this species is characterized by increased relaxivity and enhanced dichroism signal in the Soret region, suggesting a more compact heme pocket conformation. Heme binds to the folding intermediate with K-d = (1.2 +/- 0.1) x...
We report a study oil the unfolding behavior of the most abundant protein contained in plasma, human...
Human serum albumin (HSA) contains three -helical domains (I–III). The unfolding process of these do...
The changes in the far-UV CD signal, intrinsic tryptophan fluorescence and bilirubin absorbance show...
Human serum albumin (HSA) participates in heme scavenging, the bound heme turning out to be a reacti...
Human serum albumin (HSA) participates in heme scavenging, the bound heme turning out to be a reacti...
The changes in the far-UV CD signal, intrinsic tryptophan fluorescence and bilirubin absorbance show...
7-12The binding of monomeric heme to human serum albumin (HSA) was investigated using steady-state f...
The spectroscopic and reactivity properties of hemin complexes formed with cyanogen bromide fragment...
AbstractThe spectroscopic and reactivity properties of hemin complexes formed with cyanogen bromide ...
Human serum albumin (HSA), the most prominent protein in plasma, is best known for its exceptional l...
Human serum albumin (HSA), the most prominent protein in plasma, is best known for its exceptional l...
We report a study oil the unfolding behavior of the most abundant protein contained in plasma, human...
Human serum albumin (HSA) contains three -helical domains (I–III). The unfolding process of these do...
The changes in the far-UV CD signal, intrinsic tryptophan fluorescence and bilirubin absorbance show...
Human serum albumin (HSA) participates in heme scavenging, the bound heme turning out to be a reacti...
Human serum albumin (HSA) participates in heme scavenging, the bound heme turning out to be a reacti...
The changes in the far-UV CD signal, intrinsic tryptophan fluorescence and bilirubin absorbance show...
7-12The binding of monomeric heme to human serum albumin (HSA) was investigated using steady-state f...
The spectroscopic and reactivity properties of hemin complexes formed with cyanogen bromide fragment...
AbstractThe spectroscopic and reactivity properties of hemin complexes formed with cyanogen bromide ...
Human serum albumin (HSA), the most prominent protein in plasma, is best known for its exceptional l...
Human serum albumin (HSA), the most prominent protein in plasma, is best known for its exceptional l...
We report a study oil the unfolding behavior of the most abundant protein contained in plasma, human...
Human serum albumin (HSA) contains three -helical domains (I–III). The unfolding process of these do...
The changes in the far-UV CD signal, intrinsic tryptophan fluorescence and bilirubin absorbance show...