6533b7cefe1ef96bd125729e

RESEARCH PRODUCT

Quaternary transition pathway in sol–gel encapsulated haemoglobin tracked by NIR and UV spectral relaxations

Giorgio SchiròAntonio Cupane

subject

CrystallographyTransition (genetics)quaternary relaxationChemistryStereochemistryprotein dynamicchemistry.chemical_elementProtein quaternary structureStructural transitionQuaternaryOxygensol-gel encapsulationSol-gel

description

→T structural transition of haemoglobin (hb), the protein responsible for oxygen (o) transport in the red blood cells of vertebrates, is the hall mark example. This transition, which regu lates o2 uptake in the lungs and o2 release in the tissues, is a switch in the quaternary structure of the protein from a low-affinity state (T) to a high-affinity state (R), two well-characterised structures. The struc tural pathway connecting the end states of this transition remains unclear, however, although recently several experimental 1 or

10.1255/nirn.1085http://hdl.handle.net/10447/36989