Aix Marseille Univ, CNRS, Architecture et Fonction des Macromolécules Biologiques, AFMB, UMR 7257, Marseille, France.
INRAE, Aix Marseille Univ, Biodiversité et Biotechnologie Fongiques (BBF), UMR 1163, Marseille, France.
Methods Mol Biol. 2022;2449:95-147. doi: 10.1007/978-1-0716-2095-3_4.
In the last two decades it has become increasingly evident that a large number of proteins adopt either a fully or a partially disordered conformation. Intrinsically disordered proteins are ubiquitous proteins that fulfill essential biological functions while lacking a stable 3D structure. Their conformational heterogeneity is encoded by the amino acid sequence, thereby allowing intrinsically disordered proteins or regions to be recognized based on their sequence properties. The identification of disordered regions facilitates the functional annotation of proteins and is instrumental for delineating boundaries of protein domains amenable to crystallization. This chapter focuses on the methods currently employed for predicting protein disorder and identifying intrinsically disordered binding sites.
在过去的二十年中，越来越明显的是，大量的蛋白质采用完全或部分无序的构象。固有无序的蛋白质是普遍存在的蛋白质，它们在缺乏稳定的 3D 结构的情况下发挥着重要的生物学功能。它们的构象异质性由氨基酸序列编码，从而允许基于序列特性识别固有无序的蛋白质或区域。无序区域的鉴定有助于蛋白质功能的注释，并有助于划定可结晶的蛋白质域的边界。本章重点介绍目前用于预测蛋白质无序和识别固有无序结合位点的方法。
