Regulating Protein Function by Delayed Folding

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 cy...

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Bibliographic Details
Published inStructure (London) Vol. 26; no. 5; pp. 679 - 681
Main Authors Zhou, Jianhong, Dunker, A. Keith
Format Journal Article
LanguageEnglish
Published United States Elsevier Ltd 01.05.2018
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Summary: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.
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ISSN:0969-2126
1878-4186
DOI:10.1016/j.str.2018.04.011