期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 77, 期 -, 页码 -出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2022.102470
关键词
-
资金
- NIH [GM065334]
Proteins are dynamic macromolecules that exist in multiple conformational states, and their motions are essential to biological function. To better understand multidomain proteins, reweighting methods based on experimental data for elucidation of structural ensembles are needed.
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.
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