Structural stability as a probe for molecular evolution of homologous albumins studied by spectroscopy and bioinformatics.

摘要: Equilibrium unfolding by guanidinium hydrochloride (GuHCl) and urea as well evolutionary trends of two homologous albumins, pig serum albumin (PSA) rabbit (RSA), has been studied with circular dichroism, tryptophanyl fluorescence bioinformatics. GuHCl cannot distinguish the contribution electrostatic interactions to proteins which were otherwise effectively monitored urea. Higher differences in free energy changes due than show among charged amino acids are possibly responsible for higher structural stability RSA comparison PSA. From sequence HSA RSA, deletion arginine at position 117 presence one extra tryptophan 135 may possess some clue lesser Here, comparison, chemical data BSA had taken into consideration. We found that thermodynamically PSA closer BSA, respectively, accordance their homologies. Taxonomically, belongs lagomorph is hominids ungulates. Hence, on basis these thermodynamic protein denaturation different species we can use this new approach analyze phylogenetic relationship major clades eutherian mammals obtain trends.