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Evolution of the ribosomal exit tunnel through the eyes of the nascent chain
The exit tunnel is a universally conserved feature of the ribosome that directs the nascent polypeptide into the cellular environment …
Tomasz Włodarski
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Structures of protein folding intermediates on the ribosome
The ribosome biases the conformations sampled by nascent polypeptide chains along folding pathways toward biologically active states. A …
Sammy H S Chan, Julian O Streit, Tomasz Włodarski, Alkistis Mitropoulou, Anaïs M E Cassaignau, Ivana V Bukvin, Christopher A Waudby, Lisa D Cabrita, John Christodoulou
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Amyloid Forming Human Lysozyme Intermediates are Stabilized by Non‐Native Amide‐π Interactions
Mutational variants of human lysozyme cause a rare but fatal hereditary systemic amyloidosis by populating an intermediate state that …
Minkoo Ahn, Julian O Streit, Christopher A Waudby, Tomasz Włodarski, Angelo Miguel Figueiredo, John Christodoulou, Janet R Kumita
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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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