The Trigger Factor Chaperone Encapsulates and Stabilizes Partial Folds of Substrate Proteins.

ABSTRACT: How chaperones interact with protein chains to assist in their folding is a central open question in biology. Obtaining atomistic insight is challenging in particular, given the transient nature of the chaperone-substrate complexes and the large system sizes. Recent single-molecule experiments have shown that the chaperone Trigger Factor (TF) not only binds unfolded protein chains, but can also guide protein chains to their native state by interacting with partially folded structures. Here, we used all-atom MD simulations to provide atomistic insights into how Trigger Factor achieves this chaperone function. Our results indicate a crucial role for the tips of the finger-like appendages of TF in the early interactions with both unfolded chains and partially folded structures. Unfolded chain

SUBMITTER: Singhal K 

PROVIDER: S-EPMC4626277 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature