title: Simulations of disordered proteins and systems with conformational heterogeneity.
abstract: Intrinsically disordered proteins (IDPs) and protein regions can facilitate a wide variety of complex physiological processes such as binding, signaling, and formation of membraneless organelles. They can however also play pathological roles by aggregating into cytotoxic oligomers and fibrils. Characterizing the structure and function of disordered proteins is an onerous task, primarily because these proteins adopt transient structures, which are difficult to capture in experiments. Simulations have emerged as a powerful tool for interpreting and augmenting experimental measurements of IDPs. In this review we focus on computer simulations of disordered protein structures, functions, assemblies, and emerging questions that, taken together, give an overview of the field as it exists today.
authors.affiliation: Department of Chemistry and Biochemistry, University of California Santa Barbara, Santa Barbara, CA 93106, USA; Department of Physics, University of California Santa Barbara, Santa Barbara, CA 93106, USA.
authors.forename: Zachary A
authors.initials: ZA
authors.lastname: Levine
authors.affiliation: Department of Chemistry and Biochemistry, University of California Santa Barbara, Santa Barbara, CA 93106, USA; Department of Physics, University of California Santa Barbara, Santa Barbara, CA 93106, USA. Electronic address: shea@chem.ucsb.edu.
authors.forename: Joan-Emma
authors.initials: JE
authors.lastname: Shea
mesh_terms: D000682:Amyloid / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D064267:Intrinsically Disordered Proteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation
chemical_list: D000682:Amyloid; D064267:Intrinsically Disordered Proteins