Figure 1: Illustration of the pulse-chase experiment. | Nature Communications

Figure 1: Illustration of the pulse-chase experiment.

From: Accurate prediction of cellular co-translational folding indicates proteins can switch from post- to co-translational folding

Figure 1

(a) A schematic representation of the relevant protein segments of WT SFVP. Residues 1–267 correspond to the segment known as C protein. The other three protein domains are collectively referred to as p97. (b) The crystal structures of the three protein segments for which co-translational folding curves were predicted in this study. In each case, the co-translational folding domain whose behaviour is predicted is coloured blue. Top left, C protein of SFVP63. Bottom left, the FRB domain64. Right, HA1 (ref. 65), for which the co-translational folding of residues 53–275 was experimentally monitored. (c) Pulse-chase experiments proceed in a step-wise manner as described in the main text. Ribosomes (grey circles) engaged in the translation of an mRNA (light green line) incorporate radiolabelled (red dots) and unlabelled (blue dots) amino acids into nascent proteins. Only those nascent chains that contain labelled amino acids (red segments) can be experimentally observed.

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