Conformational preferences and phase behavior of intrinsically disordered low complexity sequences: insights from multiscale simulations

Kiersten M. Ruff, Rohit V. Pappu, Alex S. Holehouse

Research output: Contribution to journalReview articlepeer-review

40 Scopus citations

Abstract

While many proteins and protein regions utilize a complex repertoire of amino acids to achieve their biological function, a subset of protein sequences are enriched in a reduced set of amino acids. These so-called low complexity (LC) sequences, specifically intrinsically disordered variants of LC sequences, have been the focus of recent investigations owing to their roles in a range of biological functions, specifically phase separation. Computational studies of LC sequences have provided rich insights into their behavior both as individual proteins in dilute solutions and as the drivers and modulators of higher-order assemblies. Here, we review how simulations performed across distinct resolutions have provided different types of insights into the biological role of LC sequences.

Original languageEnglish
Pages (from-to)1-10
Number of pages10
JournalCurrent Opinion in Structural Biology
Volume56
DOIs
StatePublished - Jun 2019

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