Intrinsically disordered proteins and regions (IDPs/IDRs) constitute about one third of protein sequence space in humans and enable complex conformational and functional behaviors that underlie diverse biological processes. IDPs can function in the context of discrete multi-component assemblies but recently have been shown to undergo phase separation for form mesoscale cellular structures such as membraneless organelles and transcriptionally silent regions of chromatin. Due to their heterogeneous and transient conformations, IDPs/IDRs are challenging to characterize at atomic resolution, making it difficult to establish detailed “disorder-function relationships”. We will discuss our multidisciplinary strategies toward understanding the roles of protein disorder in regulation of apoptosis and cell division, nucleolar structure and function, and interactions with small molecules. A key goal is to illustrate the diversity and uniqueness of disorder-function relationships
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