Proteins differential scanning calorimetry

Mechanism of Crystal Growth of Protein Differential Scanning Calorimetry of Thermolysin Crystal Suspension... 

Structured proteins have also been investigated by thermal analysis [40,41], denaturing resulting in an endotherm which is readily detected by differential scanning calorimetry (DSC). DSC of recombinant resilin in the swollen state showed no transitions over a wide temperature range (25°C-140°C), further evidence of the absence of any strucmre. This is in contrast to the strucmred proteins wool and bovine serum albumin, which show denamration endotherms at 145°C and 62°C, respectively (Figure 9.6). 

Hydration of phospholipid head groups is essential properties not only for stabilizing bilayer structures in an aqueous environment, but also for fusion or endocytosis of biological membranes including protein transfers [33-35]. Hydration or swelling behavior has only been studied by indirect methods such as X-ray diffraction [36], differential scanning calorimetry (DSC) [37], and H-NMR [38,39]. 

B. Chowdhry, S. Leharne. Simulation andAnalysis of Differential Scanning Calorimetry Output Protein Unfolding Studies 1. J. Chem. Educ. 1997, 74, 236-241. 

Davio, S.R., K.M. Kienle, and B.E. Collins. 1995. Interdomain interactions in the chimeric protein toxin sCD4(178)-PE40 a differential scanning calorimetry (DSC) study. Pharm Res 12 642-648. 

Sturtevant, J.M. 1980. Differential scanning calorimetry processes involving proteins. In Bioenergetics and Thermodynamics Model Systems. A. Braibanti, editor. John Wiley Sons, New York, 391-396. 

Lepock, J.R., K.P. Ritchie, M.C. Kolios, A.M. Rodahl, K.A. Heinz, and J. Kruuv. 1992. Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation. Biochemistry 31 12706-12712. 

Brandts, J.F. and L.N. Lin. 1990. Study of strong to ultratight protein interactions using differential scanning calorimetry. Biochemistry 29 6927-6940. 

Lo, Y.L. and Y.E. Rahman. 1995. Protein location in liposomes, a drug carrier a prediction by differential scanning calorimetry. J Pharm Sci 84 805-814. 

Simulation and Analysis of Differential Scanning Calorimetry Output Protein Unfolding Studies 1 87... 

Differential scanning calorimetry is primarily used to determine changes in proteins as a function of temperature. The instrument used is a thermal analysis system, for example a Mettler DSC model 821e. The instrument coupled with a computer can quickly provide a thermal analysis of the protein solution and a control solution (no protein). The instrument contains two pans with separate heaters underneath each pan, one for the protein solution and one for the control solution that contains no protein. Each pan is heated at a predetermined equal rate. The pan with the protein will take more heat to keep the temperature of this pan increasing at the same rate of the control pan. The DSC instrument determines the amount of heat (energy) the sample pan heater has to put out to keep the rates equal. The computer graphs the temperature as a function of the difference in heat output from both pans. Through a series of equations, the heat capacity (Cp) can be determined (Freire 1995). 

The thermal unfolding of proteins is best measured by differential scanning calorimetry, which measures the heat absorbed by a protein as it is slowly heated through its melting transition (Figure 17.1). A solution of about 1 mg of protein in 1 mL of buffer and a separate reference sample of buffer alone are heated electrically.6 The additional current required to heat the protein solution is recorded. As the protein denatures, there is a large uptake of heat because the process is highly endothermic. The temperature at the maximum of the peak is... 

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