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Video: How are we so good at folding proteins?

This article discusses the complex process of protein folding, highlighting the role of ribosomes in creating proteins and their subsequent folding into functional three-dimensional shapes. It focuses on research conducted by David Balchin's lab at the Crick, emphasizing their curiosity-driven approach to understanding cellular processes at the molecular level. The study was published in 'Nature Structural & Molecular Biology' and involves insights into chaperone-assisted protein folding on the ribosome.

Proteins carry out almost every important function in our body, from copying our DNA to turning the food we eat into energy. These tiny "molecular machines" are first made by our cells as straight chains, like long pieces of string. Then, to work properly, each protein must fold into an intricate 3D shape.

The sheer scale of protein folding within our cells is staggering. Ribosomes, the molecular machines within our cells that make proteins, make about one protein every 80 seconds. Given that there are more than 5 million ribosomes in a cell, every single one of our cells makes 4 million to 8 million proteins a minute.

The remarkable process of microscopic origami is the focus of David Balchin's lab at the Crick. Balchin studied proteins and protein folding at the University of the Witwatersrand in South Africa and the Max Planck Institute of Biochemistry in Germany before starting his lab at the Crick in 2020. His team is driven by curiosity to understand the intricate workings of cells at the molecular level.

Publication details

Thomas E. Wales et al, Resolving chaperone-assisted protein folding on the ribosome at the peptide level, Nature Structural & Molecular Biology (2024). DOI: 10.1038/s41594-024-01355-x

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Lisa Lock

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Andrew Zinin

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retrieved 19 June 2026

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Source document: Resolving chaperone-assisted protein folding on the ribosome at the peptide level

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Phys.orgIndependentCenter2 days ago
Video: How are we so good at folding proteins?

This article discusses the complex process of protein folding, highlighting the role of ribosomes in creating proteins and their subsequent folding into functional three-dimensional shapes. It focuses on research conducted by David Balchin's lab at the Crick, emphasizing their curiosity-driven approach to understanding cellular processes at the molecular level. The study was published in 'Nature Structural & Molecular Biology' and involves insights into chaperone-assisted protein folding on the ribosome.

Bias read (Center): The article provides a factual overview of scientific research without taking a stance on any political issue. It focuses on biological processes and scientific inquiry, which are not inherently politically charged.

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