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Quaternary transition pathway in sol–gel encapsulated haemoglobin
tracked by NIR and UV spectral relaxations Giorgio Schirò and Antonio Cupane CNISM and Department of Physical and Astronomical Sciences,
University of Palermo, via Archirafi 36, I-90123, Palermo, Italy. E-mail: giorgio.schiro@fisica.unipa.it, cupane@fisica.unipa.it
ABSTRACT:
Conformational changes involving the
quaternary structure of proteins are of fundamental importance for several important biological mechanisms. The R→T structural transition of haemoglobin (Hb), the
protein responsible for oxygen (O2) transport in the red blood cells of vertebrates, is the hallmark example. This transition, which regulates 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.
Keywords:
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