Is Posttranslational Folding More Efficient Than Refolding from a Denatured State: A Computational Study.

ABSTRACT: The folding of proteins into their native conformation is a complex process that has been extensively studied over the past half-century. The ribosome, the molecular machine responsible for protein synthesis, is known to interact with nascent proteins, adding further complexity to the protein folding landscape. Consequently, it is unclear whether the folding pathways of proteins are conserved on and off the ribosome. The main question remains: to what extent does the ribosome help proteins fold? To address this question, we used coarse-grained molecular dynamics simulations to compare the mechanisms by which the proteins dihydrofolate reductase, type III chloramphenicol acetyltransferase, and d-alanine-d-alanine ligase B fold during and after vectorial synthesis on the ribosome to folding

SUBMITTER: Vu QV 

PROVIDER: S-EPMC10240488 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature