Datasets

Title	Accurate prediction of cellular co-translational folding indicates proteins can switch from post- to co-translational folding
Organism
Number of Samples	8
Release Date	2015/11/23 00:00
Sequencing Types
Protocol Details

GWIPS-viz	Trips-Viz
Visit GWIPS-viz

Title
Authors	Nissley DA,Sharma AK,Ahmed N,Friedrich UA,Kramer G,Bukau B,O'Brien EP
Journal	Nature communications
Publication Date	2016 Feb 18
Abstract	The rates at which domains fold and codons are translated are important factors in determining whether a nascent protein will co-translationally fold and function or misfold and malfunction. Here we develop a chemical kinetic model that calculates a protein domain's co-translational folding curve during synthesis using only the domain's bulk folding and unfolding rates and codon translation rates. We show that this model accurately predicts the course of co-translational folding measured in vivo for four different protein molecules. We then make predictions for a number of different proteins in yeast and find that synonymous codon substitutions, which change translation-elongation rates, can switch some protein domains from folding post-translationally to folding co-translationally--a result consistent with previous experimental studies. Our approach explains essential features of co-translational folding curves and predicts how varying the translation rate at different codon positions along a transcript's coding sequence affects this self-assembly process.
PMC	PMC4759629
PMID	26887592
DOI

Nissley et al. 2016 (PRJNA303186)