Deoxyhemoglobin, structure conformation

ZERBI asked whether there is any hope of detecting conformational changes in proteins by using NMR. BOVEY felt that the answer to this was yes and cited the example of oxy- and deoxyhemoglobin, where there were correlations between the changes in the NMR spectra and the quaternary structure of the protein. 

Sheh et al. (206) used X-ray crystallographic studies to design potential compounds to block the polymerization of deoxyhemoglobin S (HbS). The / 6 mutation that occurs in this protein allows one molecule (the donor) to insert itself into a hydrophobic cavity of a second molecule (the acceptor) (Figure 20). Sheh and co-workers have designed a set of cyclic peptides that mimic the loop of the donor protein which inserts into the acceptor HbS. The structure of the cyclic peptides was suggested by modeling to be such that the conformation of the peptide is close to that required by the protein loop. 

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