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ABSTRACT:
SUBMITTER: Eichmann C
PROVIDER: S-EPMC2889043 | biostudies-literature | 2010 May
REPOSITORIES: biostudies-literature
Eichmann Cédric C Preissler Steffen S Riek Roland R Deuerling Elke E
Proceedings of the National Academy of Sciences of the United States of America 20100503 20
The folding of proteins in living cells may start during their synthesis when the polypeptides emerge gradually at the ribosomal exit tunnel. However, our current understanding of cotranslational folding processes at the atomic level is limited. We employed NMR spectroscopy to monitor the conformation of the SH3 domain from alpha-spectrin at sequential stages of elongation via in vivo ribosome-arrested (15)N,(13)C-labeled nascent polypeptides. These nascent chains exposed either the entire SH3 d ...[more]