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Protein Folding on the Ribosome: Probing the Ribosomal Machinery During Biosynthesis at High Resolution
Proteins require a correct structural fold for their functionality, and consequently many diseases originate from the failure of proteins to fold productively in the cell. Folding begins co-translationally when the emerging polypeptide is still attached to its parent ribosome, and this project aims to probe the co-translational folding of polypeptides during synthesis with an emphasis on how the ribosome’s structure and chemical properties modulate this fundamental process.
Disciplines and Techniques
Project supervisor/s
Professor John Christodoulou
John's interests include: Studies of co-translational protein folding and misfolding processes on intact ribosomes, NMR studies of intact cells and Studies of intrinsically unstructured proteins involved in neurodegenerative disease.
University College London/Birkbeck University of London
Dr. Lisa Cabrita
Lisa is interested in Biochemistry and Structural Molecular Biology.
University College London
References
A structural enssemble of a ribosme-nascent chain complex during cotranslational protein folding
Nat Struct Mol Biol 23, 278-285
2016
Structural characterization of the interaction of α-synuclein nascent chains with the ribosomal surface and trigger factor
PNAS 113 (18), 5012-5017
2016
Systematic mapping of free energy landscapes of a growing filamin domain during biosynthesis
PNAS 115 (39), 9744-9749
2018
The shape of the bacterial ribosome exit tunnel affects cotranslational protein folding
eLife 7, e36326
2018
The ribosomal exit tunnel as a target for optimizing protein expression in Escherichia coli
Biotechnol J, 7 (3), 354-360
2012