Ontology highlight
ABSTRACT:
SUBMITTER: Han Y
PROVIDER: S-EPMC3411940 | biostudies-literature | 2012 Jul
REPOSITORIES: biostudies-literature
Han Yan Y David Alexandre A Liu Botao B Magadán Javier G JG Bennink Jack R JR Yewdell Jonathan W JW Qian Shu-Bing SB
Proceedings of the National Academy of Sciences of the United States of America 20120716 31
How the ribosome-bound nascent chain folds to assume its functional tertiary structure remains a central puzzle in biology. In contrast to refolding of a denatured protein, cotranslational folding is complicated by the vectorial nature of nascent chains, the frequent ribosome pausing, and the cellular crowdedness. Here, we present a strategy called folding-associated cotranslational sequencing that enables monitoring of the folding competency of nascent chains during elongation at codon resoluti ...[more]