Structure and dynamics of a ribosome-bound nascent chain by NMR spectroscopy.

ABSTRACT: Protein folding in living cells is inherently coupled to protein synthesis and chain elongation. There is considerable evidence that some nascent chains fold into their native structures in a cotranslational manner before release from the ribosome, but, despite its importance, a detailed description of such a process at the atomic level remains elusive. We show here at a residue-specific level that a nascent protein chain can reach its native tertiary structure on the ribosome. By generating translation-arrested ribosomes in which the newly synthesized polypeptide chain is selectively (13)C/(15)N-labeled, we observe, using ultrafast NMR techniques, a large number of resonances of a ribosome-bound nascent chain complex corresponding to a pair of C-terminally truncated immunoglobulin (Ig) do

SUBMITTER: Hsu ST 

PROVIDER: S-EPMC2034214 | biostudies-literature | 2007 Oct

REPOSITORIES: biostudies-literature