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Chemical Communications
Article . 2012 . Peer-reviewed
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Atomic force microscopy captures folded ribosome bound nascent chains

Authors: Anna, Loksztejn; Zackary, Scholl; Piotr E, Marszalek;

Atomic force microscopy captures folded ribosome bound nascent chains

Abstract

Direct visualization of co-translational folding of nascent polypeptide chains is challenging. Here we present, for the first time, AFM images of large protein constructs based on the membrane binding domain of ankyrin-R, complexed with the ribosome. The characteristic "horse-shoe" shape of ankyrin-R emerging from the ribosome was captured.

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Keywords

Ankyrins, Models, Molecular, Protein Folding, Protein Conformation, Escherichia coli Proteins, Microscopy, Atomic Force, Protein Structure, Tertiary, Protein Biosynthesis, Escherichia coli, Peptides, Ribosomes, Protein Binding

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    popularity
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    influence
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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
2
Average
Average
Average
bronze