Chemical Physics Program, Institute for Physical Sciences and Technology, University of Maryland, College Park, 20742, MD, USA.
Chemical Physics Program, Institute for Physical Sciences and Technology, University of Maryland, College Park, 20742, MD, USA; Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Organization, University of Maryland, College Park, 20742, MD, USA.
Curr Opin Struct Biol. 2022 Dec;77:102470. doi: 10.1016/j.sbi.2022.102470. Epub 2022 Sep 29.
Proteins are inherently dynamic macromolecules that exist in equilibrium among multiple conformational states, and motions of protein backbone and side chains are fundamental to biological function. The ability to characterize the conformational landscape is particularly important for intrinsically disordered proteins, multidomain proteins, and weakly bound complexes, where single-structure representations are inadequate. As the focus of structural biology shifts from relatively rigid macromolecules toward larger and more complex systems and molecular assemblies, there is a need for structural approaches that can paint a more realistic picture of such conformationally heterogeneous systems. Here, we review reweighting methods for elucidation of structural ensembles based on experimental data, with the focus on applications to multidomain proteins.
蛋白质是固有动态的大分子，存在于多种构象状态之间的平衡中，蛋白质主链和侧链的运动是生物功能的基础。描述构象景观的能力对于无序蛋白质、多域蛋白质和弱结合复合物尤为重要，因为单一结构表示是不充分的。随着结构生物学的研究重点从相对刚性的大分子转向更大和更复杂的系统和分子组装，需要有结构方法可以更真实地描绘这种构象异质系统。在这里，我们回顾了基于实验数据阐明结构集合的重新加权方法，重点是应用于多域蛋白质。
