Regulating Protein Function by Delayed Folding

Jianhong Zhou; A Keith Dunker

doi:10.1016/j.str.2018.04.011

Regulating Protein Function by Delayed Folding

Structure. 2018 May 1;26(5):679-681. doi: 10.1016/j.str.2018.04.011.

Authors

Jianhong Zhou¹, A Keith Dunker²

Affiliations

¹ Center for Computational Biology and Bioinformatics, Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202, USA.
² Center for Computational Biology and Bioinformatics, Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202, USA. Electronic address: kedunker@iu.edu.

PMID: 29719237
DOI: 10.1016/j.str.2018.04.011

Abstract

In this issue of Structure, Tsirigotaki et al. (2018) use bioinformatics and biophysical tools to demonstrate that many secreted proteins form long-lived, loosely packed folding intermediates. This delayed folding correlates with elevated disorder and reduced hydrophobicity compared to structured cytosolic proteins and is often stabilized by signal peptides by yet to be determined mechanisms.

Publication types

Comment

MeSH terms

Hydrophobic and Hydrophilic Interactions
Protein Folding*
Protein Sorting Signals
Proteins*

Substances

Protein Sorting Signals
Proteins