The question of which protein antigens, such as HLA class I or class II molecules, will bind, and how well, to a given antibody is often assumed to depend exclusively on the details of protein surface structure. These structures are usually based on static models resulting from X-ray crystallography. While these notions are useful, the ultimate causal factors determining how well a given antigen binds a given antibody are based in thermodynamics and can include atomic mobility and the time-varying conformations of proteins. In this article, fundamental biophysical principles of antibody-antigen interaction are discussed, concepts critical for a deeper understanding of the pertinent molecular phenomena are highlighted, and common misunderstandings are identified and debunked.

哪些蛋白质抗原（例如 HLA I 类或 II 类分子）将与给定抗体结合以及结合效果如何，通常被认为完全取决于蛋白质表面结构的细节。这些结构通常基于 X 射线晶体学产生的静态模型。虽然这些概念很有用，但决定给定抗原与给定抗体结合程度的最终因果因素是基于热力学的，并且可以包括原子迁移率和蛋白质随时间变化的构象。在本文中，讨论了抗体-抗原相互作用的基本生物物理原理，强调了对于深入理解相关分子现象至关重要的概念，并识别和揭穿了常见的误解。