锤子
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.
打开失败或需在电脑查看,请在电脑上的资料中心栏目,点击"我的下载"。建议使用手机自带浏览器。