[HTML][HTML] How the ribosome shapes cotranslational protein folding
E Samatova, AA Komar, MV Rodnina - Current Opinion in Structural Biology, 2024 - Elsevier
During protein synthesis, the growing nascent peptide chain moves inside the polypeptide
exit tunnel of the ribosome from the peptidyl transferase center towards the exit port where it …
exit tunnel of the ribosome from the peptidyl transferase center towards the exit port where it …
[HTML][HTML] Cotranslational protein folding inside the ribosome exit tunnel
OB Nilsson, R Hedman, J Marino, S Wickles, L Bischoff… - Cell reports, 2015 - cell.com
At what point during translation do proteins fold? It is well established that proteins can fold
cotranslationally outside the ribosome exit tunnel, whereas studies of folding inside the exit …
cotranslationally outside the ribosome exit tunnel, whereas studies of folding inside the exit …
Co-translational protein folding: progress and methods
M Thommen, W Holtkamp, MV Rodnina - Current opinion in structural …, 2017 - Elsevier
Highlights•Proteins begin to fold within the polypeptide exit tunnel of the
ribosome.•Ribosomes change the landscape of protein folding.•Ribosomes can stabilize …
ribosome.•Ribosomes change the landscape of protein folding.•Ribosomes can stabilize …
A switch from α‐helical to β‐strand conformation during co‐translational protein folding
X Agirrezabala, E Samatova, M Macher… - The EMBO …, 2022 - embopress.org
Cellular proteins begin to fold as they emerge from the ribosome. The folding landscape of
nascent chains is not only shaped by their amino acid sequence but also by the interactions …
nascent chains is not only shaped by their amino acid sequence but also by the interactions …
[HTML][HTML] Cotranslational folding of proteins on the ribosome
M Liutkute, E Samatova, MV Rodnina - Biomolecules, 2020 - mdpi.com
Many proteins in the cell fold cotranslationally within the restricted space of the polypeptide
exit tunnel or at the surface of the ribosome. A growing body of evidence suggests that the …
exit tunnel or at the surface of the ribosome. A growing body of evidence suggests that the …
Folding at the birth of the nascent chain: coordinating translation with co-translational folding
G Zhang, Z Ignatova - Current opinion in structural biology, 2011 - Elsevier
In the living cells, the folding of many proteins is largely believed to begin co-translationally,
during their biosynthesis at the ribosomes. In the ribosomal tunnel, the nascent peptide may …
during their biosynthesis at the ribosomes. In the ribosomal tunnel, the nascent peptide may …
The ribosomal tunnel as a functional environment for nascent polypeptide folding and translational stalling
DN Wilson, R Beckmann - Current opinion in structural biology, 2011 - Elsevier
As the nascent polypeptide chain is being synthesized, it passes through a tunnel within the
large ribosomal subunit and emerges at the solvent side where protein folding occurs …
large ribosomal subunit and emerges at the solvent side where protein folding occurs …
[HTML][HTML] Modulating co-translational protein folding by rational design and ribosome engineering
Co-translational folding is a fundamental process for the efficient biosynthesis of nascent
polypeptides that emerge through the ribosome exit tunnel. To understand how this process …
polypeptides that emerge through the ribosome exit tunnel. To understand how this process …
Transient tertiary structure formation within the ribosome exit port
The exit tunnel of the ribosome is commonly considered to be sufficiently narrow that co-
translational folding can begin only when specific segments of nascent chains are fully …
translational folding can begin only when specific segments of nascent chains are fully …
Protein folding at the exit tunnel
DV Fedyukina, S Cavagnero - Annual review of biophysics, 2011 - annualreviews.org
Over five decades of research have yielded a large body of information on how purified
proteins attain their native state when refolded in the test tube, starting from a chemically or …
proteins attain their native state when refolded in the test tube, starting from a chemically or …