方案摘要
方案下载| 应用领域 | 生物产业 |
| 检测样本 | 其他 |
| 检测项目 | |
| 参考标准 | 交互作用 |
When two proteins interact and bind, conformational changes in the proteins, and rearrangement of the solvent in the vicinity of the binding site, result in the absorption or generation of heat. Quantification of this reaction heat by ITC provides a complete thermodynamic description of the binding interaction, the stoichiometry of binding, and the association constant; in addition, if structural information is available, the contributions of specific amino acids mediating the binding event can be identified and their thermodynamic contributions quantified.
When two proteins interact and bind, conformational changes in the proteins, and rearrangement of the solvent in the vicinity of the binding site, result in the absorption or generation of heat. Quantification of this reaction heat by ITC provides a complete thermodynamic description of the binding interaction, the stoichiometry of binding, and the association constant; in addition, if structural information is available, the contributions of specific amino acids mediating the binding event can be identified and their thermodynamic contributions quantified.
利用微量热技术研究病毒结构与宿主细胞受体结合反应
等温量热法研究水泥水化
等温微量热法研究生物制品长时间稳定性评价
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