Ligand-dependent heme-protein interactions in human hemoglobin studied by Fourier transform infrared spectroscopy. Effects of quaternary structure on alpha chain tertiary structure measured at the alpha-104(G11) cysteine-SH.

Detailed measurements of the "SH vibrational absorption of a-104 cysteine in human hemoglobin and a chain dimer by Fourier transform infrared spectroscopy have been used to study the effects of heme ligation and protein quaternary structure on 01 chain tertiary structure and its role in the biological control of oxygen transport.