Single-molecule spectroscopy reveals polymer effects of disordered proteins in crowded environments.

Abstract:

:Intrinsically disordered proteins (IDPs) are involved in a wide range of regulatory processes in the cell. Owing to their flexibility, their conformations are expected to be particularly sensitive to the crowded cellular environment. Here we use single-molecule Förster resonance energy transfer to quantify the effect of crowding as mimicked by commonly used biocompatible polymers. We observe a compaction of IDPs not only with increasing concentration, but also with increasing size of the crowding agents, at variance with the predictions from scaled-particle theory, the prevalent paradigm in the field. However, the observed behavior can be explained quantitatively if the polymeric nature of both the IDPs and the crowding molecules is taken into account explicitly. Our results suggest that excluded volume interactions between overlapping biopolymers and the resulting criticality of the system can be essential contributions to the physics governing the crowded cellular milieu.

authors

Soranno A,Koenig I,Borgia MB,Hofmann H,Zosel F,Nettels D,Schuler B

doi

10.1073/pnas.1322611111

subject

Has Abstract

pub_date

2014-04-01 00:00:00

pages

4874-9

issue

13

eissn

0027-8424

issn

1091-6490

pii

1322611111

journal_volume

111

pub_type

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