Regulating Protein Function by Delayed Folding

Jianhong Zhou, A. Dunker

Research output: Contribution to journalShort survey

1 Citation (Scopus)

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. 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.

Original languageEnglish (US)
Pages (from-to)679-681
Number of pages3
JournalStructure
Volume26
Issue number5
DOIs
StatePublished - May 1 2018

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Protein Sorting Signals
Computational Biology
Hydrophobic and Hydrophilic Interactions
Proteins

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

Regulating Protein Function by Delayed Folding. / Zhou, Jianhong; Dunker, A.

In: Structure, Vol. 26, No. 5, 01.05.2018, p. 679-681.

Research output: Contribution to journalShort survey

Zhou, Jianhong ; Dunker, A. / Regulating Protein Function by Delayed Folding. In: Structure. 2018 ; Vol. 26, No. 5. pp. 679-681.
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