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… Click to show full 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.
               
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