Adedayo Fodeke

Name: Adedayo A. Fodeke

Rank: Lecturer I

Office: Room G20 (Ground Floor, White house), Department of Chemistry, OAU, Ile-Ife.


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Adedayo Fodeke holds a PhD degree in Biophysical Chemistry from the University of Ibadan, Nigeria. His research focus is on protein structure and effect of cellular environment of protein structure. This is with a view to relating the structural changes caused by the environment in which protein are found on their functional behaviour (pathological and beneficial). He was a visiting research fellow at the National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health. USA. He is currently a Lecturer I at the Department of Chemistry, Obafemi Awolowo University.    

 Area of Specialization / Research Interest: Biophysical Chemistry

Selected Publications:

(i)         Fodeke, A. A., Aboluwoye C. O and Okonjo, K. O. (2005) Electrostatic effects of ionisable groups on the reactivity of the CysF9[93]β sulphydryl group in haemoglobins. Ife Journal of Science 7 (2): 229 – 236                      

 (ii)       Okonjo, K. O and Fodeke, A. A. (2006). Reversible reaction of 5,5′-dithiobis(2-nitrobenzoate) with the hemoglobins of the domestic cat: Acetylation of NH3+ terminal group of the β chain transforms complex pH dependence of the forward apparent second order rate constant to a simple form. Biophysical Chemistry 119 (2): 196 – 204                                                                    

(iii)       Okonjo, K. O., Fodeke A. A. and Kehinde, A. T, (2006). Reversible reaction of 5,5’-dithiobis(2-nitrobenzoate) with the CysF9[93]β sulfhydryl groups of the hemoglobins of the domestic cat: Variation of the equilibrium and reverse rate constants with pH. Biophysical Chemistry 121 (1):  61 – 73                         

(iv)       Okonjo K. O., Adediji A. T., Fodeke A. A., Adeboye O. and Ezeh C. V. (2007) Transition of hemoglobin between two tertiary conformations: Determination of equilibrium and thermodynamic parameters from the reaction of 5,5′-dithiobis(2-nitrobenzoate) with the CysF9[93]β sulfhydryl group. Biophysical Chemistry 128, 56 – 62.                                                                                                                         

 (v)        Fodeke, A. A. and Minton A. P (2010) Quantitative characterization of polymer-polymer, protein-protein, and polymer-protein interaction via tracer sedimentation equilibrium. Journal of Physical Chemistry B. 114, 10876 – 10880  USA

 (vi)      Fodeke, A. A. and Minton A. P (2011) Quantitative characterization of Temperature-Independent and Temperature-Dependent Protein-Protein Interactions in Highly Nonideal Solutions. Journal Physical Chemistry B. 115 (38) 11261 – 11268

(vii)     Fodeke, A. A. and Minton A. P. (2013) Aldolase in Concentrated Ficoll 70 Solution: Analysis with Scaled Particle Theory. Ife Journal of Science 15 (2) 399 – 407                                                                                                                                   

(viii)    Okonjo, K. O. Olatunde M. O., Fodeke A. A., Babalola J. O (2014)  Bohr effect of human hemoglobin A: magnitude of negative contributions determined by the equilibrium between two tertiary structures. Biophysical Chemistry (190 – 191) 41 – 49.

(ix)       Fodeke, A. A., Babalola J. O., Aboluwoye C. O.  (2016) Effect of High Ionic Strength and Inositol Hexakisphosphate on the Reactivity of CysF9[93]β of  Rabbit Haemoglobin. International Journal of Basic and Applied Sciences 5 (3) 86 – 95                        

(x)     Fodeke, A. A., Oyedare K. O.  Babalola J. O. (2016) Tertiary level r ↔t isomerization significantly raises the pKa of CysF9[93]β linked ionizable groups of straw-coloured fruit bat hemoglobin: Variation of apparent forward second-order rate constant with pH. International Journal of Life Sciences 5 (3) 171 – 179

(xi)     Fodeke, A. A. (2017) Organic Phosphate Binding Inhibits High pH t-isomerization of the β-Chain in Straw-coloured Fruit Bat (Eidolon helvum) Hemoglobin. South African Journal of Chemistry, 70 181 – 188