NANO等温差示扫描量热仪

In the past few decades calcium sulfate based building products have become materials of choice for various interior construction purposes, The basis of gypsum technology is the ability of gypsum to transform into various calcium sulfates (hemihydrale, anhydrite) when being heated. When hemihydrate or anhydrite is mixed with water calcium sulfale dihydrate is formed again due to re-hydralion. During re-hydration of hemihydrate, the following exothermic reaction occurs:

The development of monoclonal antibody (Mab) based drugs has undergone considerable growth since the release of the first Mab in the mid-eighties. Intuitive biophysical tools that examine and quantify interactions and conformational dynamics are important in demonstrating and understanding local and global conformational changes. The structure of antibodies as well as other macromolecules is related to its function and efficacy therefore control over these parameters is essential. The association of antigens to antibodies or of antibodies to delivery assemblies such as liposomes or gold nanoparticles can be addressed by isothermal titration calorimetry (ITC) while the folding of antibodies can be assayed using differential scanning calorimetry (DSC). Both techniques offer the advantage of using native solutions and both instruments are offered by TA Instruments.

通过差示扫描量热仪（DSC）使用CSC Nano-DSC III测定蛋白质的热力学参数，需要大量相同的蛋白质做表面等离子体共振或荧光研究。由于Nano-DSC III 高度的敏感性和基线重复性，以及样品池的小体积(300 μL)和毛细管配置（能够延迟不可逆的蛋白质聚合和沉淀），一个完整的、可判断的、准确的扫描可以得到基本上所有的想要测试的蛋白质。?

Various techniques yield either structural or functional information about a protein, but DSC uniquely provides insights into both the three-dimensional arrangement and the functional properties of a protein’s structural components.

DSC is the most direct and sensitive approach for characterizing the thermodynamic parameters controlling noncovalent bond formation (and therefore stability) in proteins and other macromolecules. In an experiment requiring only a few micrograms of material, the protein is thermally unfolded, allowing the relationship between enthalpy and entropy of the denaturation process to be established in about one hour. Correlating thermodynamic properties to stability is necessary for the rational design of engineered proteins and protein therapeutics.

Although membrane proteins are very difficult to work with, ultra-sensitive calorimetry can over-come the limitations of many other physical characterization techniques to provide insights into the factors driving membrane protein/lipid assembly and controlling the stability of the conplexes.

Although membrane proteins are very difficult to work with, ultra-sensitive calorimetry can overcome the limitations of many other physical characterization techniques to provide insights into the factors driving membrane protein/lipid assembly and controlling the stability of the complexes.

Like ITC, DSC is a valuable approach for studying binding between a biological macromolecule and a ligand such as another biopolymer or a drug. Unlike ITC, DSC allows the thermodynamics that drive binding to be correlated, at least to a degree, with conformational changes in the macromolecule caused by the binding reaction. DSC is particularly useful for characterizing very tight or slow binding interactions. DSC also allows characterization of binding reactions that are incompatible with the organic solvent requirements of some ITC experiments (i.e., where ligand solubility for an ITC experiment requires concentrations of organic solvent not tolerated by the protein).?