Reply to Jensen and Blackledge: Dual quantifications of intrinsically disordered proteins by NMR ensembles and molecular dynamics simulations
- PMID: 24877227
- PMCID: PMC4000842
- DOI: 10.1073/pnas.1400340111
Reply to Jensen and Blackledge: Dual quantifications of intrinsically disordered proteins by NMR ensembles and molecular dynamics simulations
Conflict of interest statement
The authors declare no conflict of interest.
Comment on
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Multiscaled exploration of coupled folding and binding of an intrinsically disordered molecular recognition element in measles virus nucleoprotein.Proc Natl Acad Sci U S A. 2013 Oct 1;110(40):E3743-52. doi: 10.1073/pnas.1308381110. Epub 2013 Sep 16. Proc Natl Acad Sci U S A. 2013. PMID: 24043820 Free PMC article.
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Testing the validity of ensemble descriptions of intrinsically disordered proteins.Proc Natl Acad Sci U S A. 2014 Apr 22;111(16):E1557-8. doi: 10.1073/pnas.1323876111. Epub 2014 Mar 17. Proc Natl Acad Sci U S A. 2014. PMID: 24639541 Free PMC article. No abstract available.
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Multiscaled exploration of coupled folding and binding of an intrinsically disordered molecular recognition element in measles virus nucleoprotein.Proc Natl Acad Sci U S A. 2013 Oct 1;110(40):E3743-52. doi: 10.1073/pnas.1308381110. Epub 2013 Sep 16. Proc Natl Acad Sci U S A. 2013. PMID: 24043820 Free PMC article.
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References
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- Lindorff-Larsen K, Trbovic N, Maragakis P, Piana S, Shaw DE. Structure and dynamics of an unfolded protein examined by molecular dynamics simulation. J Am Chem Soc. 2012;134(8):3787–3791. - PubMed
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