کاربرد DSC در تعیین دمینهای پرونئین

عنوان انگليسی

Application of DSC in detection of protein Domains

خلاصه انگلیسی

Differential Scanning calorimetry is a powerful tool in study of protein stability and its thermodynamics since it directly measures enthalpy of protein denaturation. By the structural view Protein domain is a part of protein sequence that can evolve, function, and exist independently of the rest of the protein chain. Each domain forms a compact three-dimensional structure and often can be independently stable and folded. Each domain exerts a special function to the protein, such as an enzyme's active site, which binds the substrate to the enzyme. In Biophysical chemistry we consider protein domain as "Independently folding structural unit". Gaining the information about the protein domains has great value in biotechnology and protein stability. Depending on protein properties and environment conditions, protein thermal denaturation can be reversible or irreversible. More than 90% of proteins undergo the irreversible denaturation process. Protein domain detection is based on its behavior under thermal unfolding. Mainly for proteins which unfold reversibly, protein domain detection carried out by deconvolution of excess molar heat capacity profile. We successfully could determine the structural domains of Euphorbia Latex Amine oxidase using DSC profiles of modified ELAO. The major method for domain detection of proteins undergoing irreversible denaturation is the successive annealing method. In this method the sample heated repeatedly 1-2oC above the predicted transitions. This method has been used for the calorimetric analysis of proteins like sub-fragment1 of myosin Zn2+-complex of α-Lactalbumin. But the relations between the energetic and structural domains have not been clarified yet and needs more investigation

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