动能
过程(计算)
化学
计算机科学
生物系统
物理
生物
量子力学
操作系统
作者
Aki Tanabe,Kouhei Tsumoto
标识
DOI:10.1007/978-1-0716-2609-2_23
摘要
In the computational design of antibodies, the interaction analysis between target antigen and antibody is an essential process to obtain feedback for validation and optimization of the design. Kinetic and thermodynamic parameters as well as binding affinity (KD) allow for a more detailed evaluation and understanding of the molecular recognition. In this chapter, we summarize the conventional experimental methods which can calculate KD value (ELISA, FP), analyze a binding activity to actual cells (FCM), and evaluate the kinetic and thermodynamic parameters (ITC, SPR, BLI), including high-throughput analysis and a recently developed experimental technique.
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