David Balchin
@davidbalchin.bsky.social
Group leader at the Francis Crick institute and head of the Protein Biogenesis lab. Interested in protein folding, ribosomes and molecular chaperones.
A hidden hydrophobic groove on the ribosome surface, normally capped by a flexible "lid", can stabilise nascent amphipathic helices and change the pathway of domain folding.
June 2, 2025 at 4:12 PM
A hidden hydrophobic groove on the ribosome surface, normally capped by a flexible "lid", can stabilise nascent amphipathic helices and change the pathway of domain folding.
New from our lab @crick.ac.uk, in collaboration with the Enchev and Bukau labs.
By studying a protein that is difficult to fold, we discover fascinating new mechanisms by which the ribosome supports protein biogenesis.
www.biorxiv.org/content/10.1...
By studying a protein that is difficult to fold, we discover fascinating new mechanisms by which the ribosome supports protein biogenesis.
www.biorxiv.org/content/10.1...
June 2, 2025 at 4:12 PM
New from our lab @crick.ac.uk, in collaboration with the Enchev and Bukau labs.
By studying a protein that is difficult to fold, we discover fascinating new mechanisms by which the ribosome supports protein biogenesis.
www.biorxiv.org/content/10.1...
By studying a protein that is difficult to fold, we discover fascinating new mechanisms by which the ribosome supports protein biogenesis.
www.biorxiv.org/content/10.1...
A hidden hydrophobic groove on the ribosome surface, normally capped by a flexible "lid", can stabilise nascent amphipathic helices and change the pathway of domain folding.
June 2, 2025 at 4:06 PM
A hidden hydrophobic groove on the ribosome surface, normally capped by a flexible "lid", can stabilise nascent amphipathic helices and change the pathway of domain folding.