This study compared the molecular dynamics (MD) of haemoglobin (Hb) bound to haeme in humans, camels, and bovines. The camel haemoglobin alpha and beta subunits showed larger amino acid differences, compared with bovine and human Hb. The bovine Hb was more phylogenetically related to human Hb than camel Hb. The camel haemoglobin structure complexed with haeme showed the highest stability by showing the lowest root mean square deviations (RMSD) and root mean square fluctuations (RMSF), compared with bovine and human structures. The Molecular Mechanics/Poisson Boltzman Surface Area (MM/PBSA) method was used to estimate the binding potency of haeme with the studied Hbs. The binding free energy of haeme was calculated to be -688.062 for bovines, -897.019 for camels, and -585.291 for humans. As a consequence, camel Hb had the highest binding potency, followed by bovines, and then humans. The structure and binding features of camel Hb contributes to its role in adaptation to dehydration and the harsh environment by adopting of higher affinity for haeme.
Key words: Camel, haemoglobin, haeme, molecular dynamics
Home