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The ribosome lowers the entropic penalty of protein folding.
Most proteins fold during biosynthesis on the ribosome1, and co-translational folding energetics, pathways and outcomes of many …
Julian O Streit, Ivana V Bukvin, Sammy HS Chan, Shahzad Bashir, Lauren F Woodburn, Tomasz Włodarski, Angelo M Figueiredo, Gabija Jurkeviciute, Haneesh K Sidhu, Charity R Hornby, Christopher A Waudby, Lisa D Cabrita, Anaïs ME Cassaignau, John Christodoulou
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Bayesian reweighting of biomolecular structural ensembles using heterogeneous cryo-EM maps with the cryoENsemble method.
Cryogenic electron microscopy (cryo-EM) has emerged as a powerful method for the determination of structures of complex biological …
Tomasz Włodarski, Julian O Streit, Alkistis Mitropoulou, Lisa D Cabrita, John Christodoulou
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The ribosome stabilizes partially folded intermediates of a nascent multi-domain protein.
Co-translational folding is crucial to ensure the production of biologically active proteins. The ribosome can alter the folding …
Sammy H S Chan, Tomasz Włodarski, Julian O Streit, Anaïs M E Cassaignau, Lauren F Woodburn, Minkoo Ahn, Georg Johannes Freiherr von Sass, Christopher A Waudby, Nediljko Budisa, Lisa D Cabrita, John Christodoulou
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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 …
Minkoo Ahn, Tomasz Włodarski, Alkistis Mitropoulou, Sammy H S Chan, Haneesh Sidhu, Elena Plessa, Thomas A Becker, Nediljko Budisa, Christopher A Waudby, Roland Beckmann, Anaïs M E Cassaignau, Lisa D Cabrita, John Christodoulou
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Common sequence motifs of nascent chains engage the ribosome surface and trigger factor.
In the cell, the conformations of nascent polypeptide chains during translation are modulated by both the ribosome and its associated …
Annika Deckert, Anaïs M E Cassaignau, Xiaolin Wang, Tomasz Włodarski, Sammy H S Chan, Christopher A Waudby, John P Kirkpatrick, Michele Vendruscolo, Lisa D Cabrita, John Christodoulou
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Interactions between nascent proteins and the ribosome surface inhibit co-translational folding.
Most proteins begin to fold during biosynthesis on the ribosome. It has been suggested that interactions between the emerging …
Anaïs M E Cassaignau, Tomasz Włodarski, Sammy H S Chan, Lauren F Woodburn, Ivana V Bukvin, Julian O Streit, Lisa D Cabrita, Christopher A Waudby, John Christodoulou
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Nascent chain dynamics and ribosome interactions within folded ribosome-nascent chain complexes observed by NMR spectroscopy.
The folding of many proteins can begin during biosynthesis on the ribosome and can be modulated by the ribosome itself. Such …
Charles Burridge, Christopher A Waudby, Tomasz Włodarski, Anaïs M E Cassaignau, Lisa D Cabrita, John Christodoulou
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Visualising nascent chain dynamics at the ribosome exit tunnel by cryo-electron microscopy
One of the important questions in protein synthesis on the ribosome is how the nascent polypeptide chains fold during translation. …
Abid Javed, Lisa D. Cabrita, Anaïs M.E. Cassaignau, Tomasz Włodarski, John Christodoulou, Elena V. Orlova
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Systematic mapping of free energy landscapes of a growing filamin domain during biosynthesis.
Cotranslational folding (CTF) is a fundamental molecular process that ensures efficient protein biosynthesis and minimizes the …
Christopher A Waudby, Tomasz Włodarski, Maria-Evangelia Karyadi, Anaïs M E Cassaignau, Sammy H S Chan, Anne S Wentink, Julian M Schmidt-Engler, Carlo Camilloni, Michele Vendruscolo, Lisa D Cabrita, John Christodoulou
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Evolutionary interplay between structure, energy and epistasis in the coat protein of the ϕX174 phage family.
Viral capsids are structurally constrained by interactions among the amino acids (AAs) of their constituent proteins. Therefore, …
Rodrigo A F Redondo, Harold P de Vladar, Tomasz Włodarski, Jonathan P Bollback
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