[HTML][HTML] NMR structure of the α-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding
CM Santiveri, JM Pérez-Canadillas… - Journal of Biological …, 2004 - ASBMB
The structure of α-hemoglobin stabilizing protein (AHSP), a molecular chaperone for free α-
hemoglobin, has been determined using NMR spectroscopy. The protein native state shows
conformational heterogeneity attributable to the isomerization of the peptide bond preceding
a conserved proline residue. The two equally populated cis and trans forms both adopt an
elongated antiparallel three α-helix bundle fold but display major differences in the loop
between the first two helices and at the C terminus of helix 3. Proline to alanine single point …
hemoglobin, has been determined using NMR spectroscopy. The protein native state shows
conformational heterogeneity attributable to the isomerization of the peptide bond preceding
a conserved proline residue. The two equally populated cis and trans forms both adopt an
elongated antiparallel three α-helix bundle fold but display major differences in the loop
between the first two helices and at the C terminus of helix 3. Proline to alanine single point …