Physics-based computational and theoretical approaches to intrinsically disordered proteins. Academic Article

abstract

• Intrinsically disordered proteins (IDPs) are an important class of proteins that do not fold to a well-defined three-dimensional shape but rather adopt an ensemble of inter-converting conformations. This feature makes their experimental characterization challenging and invites a theoretical and computational approach to complement experimental studies. In this review, we highlight the recent progress in developing new computational and theoretical approaches to study the structure and dynamics of monomeric and order higher assemblies of IDPs, with a particular emphasis on their phase separation into protein-rich condensates.

authors

• Mittal, Jeetain

published proceedings

• Curr Opin Struct Biol

altmetric score

• 19.2

author list (cited authors)

• Shea, J., Best, R. B., & Mittal, J.

citation count

• 36

complete list of authors

• Shea, Joan-Emma||Best, Robert B||Mittal, Jeetain

publication date

• April 2021

publisher

• Elsevier  Publisher

published in

• Current Opinion in Structural Biology  Journal

keywords

• Intrinsically Disordered Proteins
• Physics
• Protein Conformation

PubMed Central ID

• 33545530

Digital Object Identifier (DOI)

• 10.1016/j.sbi.2020.12.012

start page

• 219

end page

• 225

volume

• 67

URL

• http://dx.doi.org/10.1016/j.sbi.2020.12.012