The HD-exchange motions of ribosomal protein S6 are insensitive to reversal of the protein-folding pathway.

ABSTRACT: An increasing number of protein structures are found to encompass multiple folding nuclei, allowing their structures to be formed by several competing pathways. A typical example is the ribosomal protein S6, which comprises two folding nuclei (sigma1 and sigma2) defining two competing pathways in the folding energy landscape: sigma1 --> sigma2 and sigma2 --> sigma1. The balance between the two pathways, and thus the order of folding events, is easily controlled by circular permutation. In this study, we make use of this ability to manipulate the folding pathway to demonstrate that the dynamic motions of the S6 structure are independent of how the protein folds. The HD-exchange protection factors remain the same upon complete reversal of the folding order. The phenomenon arises because the

SUBMITTER: Haglund E 

PROVIDER: S-EPMC2799792 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature