Probing ribosome-nascent chain complexes produced in vivo by NMR spectroscopy.

ABSTRACT: The means by which a polypeptide chain acquires its unique 3-D structure is a fundamental question in biology. During its synthesis on the ribosome, a nascent chain (NC) emerges vectorially and will begin to fold in a cotranslational fashion. The complex environment of the cell, coupled with the gradual emergence of the ribosome-tethered NC during its synthesis, imposes conformational restraints on its folding landscape that differ from those placed on an isolated protein when stimulated to fold following denaturation in solution. To begin to examine cotranslational folding as it would occur within a cell, we produce highly selective, isotopically labeled NCs bound to isotopically silent ribosomes in vivo. We then apply NMR spectroscopy to study, at a residue specific level, the conformati

SUBMITTER: Cabrita LD 

PROVIDER: S-EPMC2799734 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature