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  Co-translational protein folding: Progress and methods.

Thommen, M., Holtkamp, W., & Rodnina, M. V. (2017). Co-translational protein folding: Progress and methods. Current Opinion in Structural Biology, 42, 83-89. doi:10.1016/j.sbi.2016.11.020.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-34CF-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-34D5-9
Genre: Journal Article

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2380693.pdf (Publisher version), 836KB
 
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 Creators:
Thommen, M.1, Author              
Holtkamp, W.1, Author              
Rodnina, M. V.1, Author              
Affiliations:
1Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578598              

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 Abstract: Proteins are synthesized as linear polymers and have to fold into their native structure to fulfil various functions in the cell. Folding can start co-translationally when the emerging peptide is still attached to the ribosome and is guided by the environment of the polypeptide exit tunnel and the kinetics of translation. Major questions are: When does co-translational folding begin? What is the role of the ribosome in guiding the nascent peptide towards its native structure? How does translation elongation kinetics modulate protein folding? Here we suggest how novel structural and biophysical approaches can help to probe the interplay between the ribosome and the emerging peptide and present future challenges in understanding co-translational folding.

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Language(s): eng - English
 Dates: 2016-12-092017-02
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.sbi.2016.11.020
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Title: Current Opinion in Structural Biology
Source Genre: Journal
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Pages: - Volume / Issue: 42 Sequence Number: - Start / End Page: 83 - 89 Identifier: -