Large oligomeric proteins constitute a major fraction of proteomes, but are difficult to refold in vitro, raising the question of how cells direct their biogenesis. Roeselová and Shivakumaraswamy et a...

Nature Protocols, Published online: 12 January 2026; doi:10.1038/s41596-025-01279-wA strategy for isolating Escherichia coli ribosome–nascent chain complexes and analyzing their conformational dynamics and interactors at peptide level using hydrogen–deuterium exchange mass spectrometry is presented.

The GroEL/ES chaperonin can act during protein synthesis to promote folding. Here, Roeselová et al. show how GroEL captures, remodels and sequesters nascent proteins in its central chamber, while they...

Nature Structural & Molecular Biology, Published online: 19 September 2025; doi:10.1038/s41594-025-01676-5By studying dynamic folding intermediates on the human ribosome, Pellowe et al. show that newly made domains help each other to fold but do not stably interact until synthesis is complete, avoiding interdomain misfolding.

PhD Project - Delineating stages of Aquaporin biogenesis at Aston University, listed on FindAPhD.com

Proteins with multiple domains are intrinsically prone to misfold, yet fold efficiently during their

PhD Project - Delineating stages of Aquaporin biogenesis at Aston University, listed on FindAPhD.com