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Protein Folding on the Ribosome
Interaction of α-synuclein nascent chains with the ribosomal surface and trigger factor
TITAN: 2D NMR lineshape analysis
A powerful new analysis of NMR titration data, with easy to use software. Find out more.
A structural ensemble of a ribosome-nascent chain complex
Our NSMB article describes the comprehensive characterisation of the co-translational folding of the FLN5 immunoglobulin domain.
A strategy for studying co-translational folding by NMR spectroscopy
Read the latest on our experimental approaches in Nature Protocols.
Our research
As nascent chains emerge from the ribosomal exit tunnel and into the cellular environment, the majority must fold into specific structures in order to function. Knowledge of how this folding process occurs, and how misfolding is avoided, is central to our understanding of living systems.
We use NMR spectroscopy together with biochemical and biophysical methods to study these co-translational folding processes with atomic resolution, in order to understand the fundamental principles of folding and misfolding within the cellular environment.
