Single-molecule fluorescence studies of intrinsically disordered proteins and liquid phase separation

5Citations
Citations of this article
55Readers
Mendeley users who have this article in their library.

Abstract

Intrinsically disordered proteins (IDPs) are ubiquitous in proteomes and serve in a range of cellular functions including signaling, regulation, transport and enzyme function. IDP misfunction and aggregation are also associated with several diseases including neurodegenerative diseases and cancer. During the past decade, single-molecule methods have become popular for detailed biophysical and structural studies of these complex proteins. This work has included recent applications to cellular liquid-liquid phase separation (LLPS), relevant for functional dynamics of membraneless organelles such as the nucleolus and stress granules. In this concise review, we cover the conceptual motivations for development and application of single-molecule fluorescence methods for such IDP studies. We follow with a few key examples of systems and biophysical problems that have been addressed, and conclude with thoughts for emerging and future directions.

Cite

CITATION STYLE

APA

Nasir, I., Onuchic, P. L., Labra, S. R., & Deniz, A. A. (2019, October 1). Single-molecule fluorescence studies of intrinsically disordered proteins and liquid phase separation. Biochimica et Biophysica Acta - Proteins and Proteomics. Elsevier B.V. https://doi.org/10.1016/j.bbapap.2019.04.007

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free