Abstract
Human serum albumin (HAS) plays important roles in the body including transport of different ions, fatty acids, drugs, hormones and metabolites. This protein has a key role in regulation of blood osmotic pressure. In correspond to the wide variations of functional aspects of HSA, its structure is characterized by various conformations. In this study, HSA behavior during denaturation and conformational changes in presence of flouxetine and cortisol (as ligands) at 37oC and 42oC temperatures is studied by using pH metery denaturation, UV spectroscopy, florescence spectroscopy, and circular dichroism (CD) techniques. Differential scanning calorimetery profiles of HSA in the absence and presence of ligands are also provided and have been analyzed. Complicated statistical analysis shows the existence of several fine structures features for HSA. This ability of HSA for structural switching corresponds to potent potential of albumin for doing various functions. The finding can be attributed to the other similar proteins by additional investigations.Keywords: Human Serum Albumin, Conformation, Fine Structural Features, Conformer and Denaturation
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