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(*) Summary. Haemoglobin is the most studied protein, yet it remains evergreen because of the lack of agreement on the mechanisms underlying the fine regulations of its structural and functional properties. The x-ray crystallographic studies on the protein could only reveal its static structure whereas its functions depend on it dynamic structure in solution. The nuclear magnetic resonance studies of the protein generate data which are often too complex to analyse. Hence, the need to find other methods of getting information on structural changes of haemoglobin in solution; its sulphydryl reactivity is apparently one of the methods.
Sulphydryl groups are the most reactive functional group in the non-haem part of haemoglobin. The CysF3[93]β is invariant in haemoglobin and is an indicator for tertiary and quaternary structure change in haemoglobin. Its reactivity is influenced by allosteric effectors such as the proton (H+) and inositol hexakisphosphate (inositol-P6).
Using kinetics as a tool, the reactivity sulphydryl group has been used to determine the tetramer-dimer equilibrium constant and consequently the Bohr Effect of haemoglobin. The electrostatic environment of the sulphydryl groups has been explored to interpret the structure of avian and mammal haemoglobins in solution. Significant differences has been found between the structures of avian and mammal haemoglobins. Experimental data has been used to justify the need for second haemoglobin for animals that have them. The role of salt-bridges in moderating the structural changes for functional properties of haemoglobin has been determined. A combination of kinetic and equilibrium data has been used to quantify the tertiary states of the macromolecule and the factors that shifts the equilibrium.

(**) Biodata. Dr. Jonathan Oyebamiji Babalola is a Reader and Sub-Dean (Sciences), Postgraduate School, University of Ibadan, Nigeria. His research interest is in reactivity of haemoglobin and dynamics of lipid transfer/membrane fusion. Dr Babalola holds a bachelors degree (Chemistry) of Obafemi Awolowo University, Ile-Ife, Nigeria. He got his M.Sc. (Physical Chemistry) and Ph.D (Biophysical Chemistry) from University of Ibadan, Nigeria in 1993 and 1999 respectively. He has a number of academic fellowships to his credit; he was a TRIL fellow, TWAS Associate, Pilot Associate of Organisation for Prohibition of Chemical Weapons, The Hague, fellow of ICSU-Jawaral Nehru Centre for Advance Scientific Research, Deutsch Academic Exchanges Services (DAAD), Alexander von Humboldt Stiftung, Bonn, Germany and Safety Training Fellow of the International Union for Pure and Applied Chemistry (IUPAC). He has supervised four Ph.D. students and about twenty master students. He has published widely in both international and national peer-reviewed journals.