Optimal design of adaptively sampled NMR experiments for measurement of methyl group dynamics with application to a ribosome-nascent chain complex-Reference-Cited by-同舟云学术

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Optimal design of adaptively sampled NMR experiments for measurement of methyl group dynamics with application to a ribosome-nascent chain complex

Published:2021-05 Issue: Volume:326 Page:106937
ISSN:1090-7807
Container-title:Journal of Magnetic Resonance
language:en
Short-container-title:Journal of Magnetic Resonance

Author:

Waudby Christopher A.^ORCID,Burridge Charles^ORCID,Christodoulou John^ORCID

Funder

National Institute of General Medical Sciences

Wellcome Trust

Medical Research Council

Biotechnology and Biological Sciences Research Council

Cancer Research UK

National Institutes of Health

Publisher

Elsevier BV

Subject

Condensed Matter Physics,Nuclear and High Energy Physics,Biochemistry,Biophysics

Reference50 articles.

1. Protein misfolding, amyloid formation, and human disease: a summary of progress over the last decade;Chiti;Annu. Rev. Biochem.,2017

2. In vivo aspects of protein folding and quality control;Balchin;Science,2016

3. How does the ribosome fold the proteome?;Cassaignau;Annu. Rev. Biochem.,2020

4. Nature and Regulation of protein folding on the ribosome;Waudby;Trends Biochem. Sci.,2019

5. The ribosome modulates nascent protein folding;Kaiser;Science,2011

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1. The ribosome lowers the entropic penalty of protein folding;Nature;2024-08-07

2. How protein fold: Insights from nuclear magnetic resonance spectroscopy;Encyclopedia of Condensed Matter Physics;2024

3. An introduction to one- and two-dimensional lineshape analysis of chemically exchanging systems;Journal of Magnetic Resonance Open;2023-12

4. Nascent Chains Derived from a Foldable Protein Sequence Interact with Specific Ribosomal Surface Sites near the Exit Tunnel;2023-04-13

5. Nascent-Chain Interaction Networks and Their Effect on the Bacterial Ribosome;2022-11-01

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