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Explore a selection of research case studies from the past five years.

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Researchers at the Crick are tackling the big questions about human health and disease, and new findings are published every week.

Our faculty have picked some of the most significant papers published by Crick scientists, all of which are freely available thanks to our open science policy.

Year published

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A cartoon of protein folding during translation at the ribosome.

Only connect (carefully): how complex proteins fold correctly

Complicated proteins with multiple domains could easily misfold, but the ribosome, where proteins are made, somehow folds them properly. Two teams at the Crick used advanced imaging and chemical techniques to see how the ribosome manages this feat in human cells. They found that protein subdomains fold progressively as they are made, with flexible ends preventing the growing complex from locking in to its final conformation until the complete protein has been made. This controlled timing helps avoid misfolding. Unlike bacteria, where domains connect early and stay fixed, human ribosomes delay these connections, probably to ensure complex, multidomain proteins form correctly.

The human ribosome modulates multidomain protein biogenesis by delaying cotranslational domain docking

Published in Nature Structural & Molecular Biology

Published

A cartoon of protein folding during translation at the ribosome.

Molecular origami: how cells fold proteins correctly

Properly folding all the proteins manufactured in a cell is crucial for all biological functions, but despite billions of years of evolution in which to perfect the process, proteins often misfold. Molecular chaperones assist the folding process during protein synthesis, but how chaperones work together to recognise nascent protein chains and enable correct folding is not well understood. The Balchin lab at the Crick, in collaboration with the Chemical Biology, Structural Biology and Proteomics teams, has now used advanced mass spectrometry techniques to explore how complex, multidomain proteins fold during synthesis. Their study shows how different classes of chaperone interact with and protect proteins at different stages of folding, and sets the stage for further insights into how sequential, coordinated chaperone action during protein synthesis assists in maintaining healthy cells.

Mechanism of chaperone coordination during cotranslational protein folding in bacteria

Published in Molecular Cell

Published

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Research case studies 

Explore a selection of recent case studies that spotlight particular areas of research at the Crick.