Reply to Jensen and Blackledge: Dual quantifications of intrinsically disordered proteins by NMR ensembles and molecular dynamics simulations

Comment

Yong Wang et al. Proc Natl Acad Sci U S A. 2014.

. 2014 Apr 22;111(16):E1559.

doi: 10.1073/pnas.1400340111.

No abstract available

Conflict of interest statement

The authors declare no conflict of interest.

Multiscaled exploration of coupled folding and binding of an intrinsically disordered molecular recognition element in measles virus nucleoprotein.
Wang Y, Chu X, Longhi S, Roche P, Han W, Wang E, Wang J. Wang Y, et al. 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.
Testing the validity of ensemble descriptions of intrinsically disordered proteins.
Jensen MR, Blackledge M. Jensen MR, et al. 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.

1. Jensen MR, Blackledge M. Testing the validity of ensemble descriptions of intrinsically disordered proteins. Proc Natl Acad Sci USA. 2014;111:E1557–E1558. - PMC - PubMed
1. Wang Y, et al. Multiscaled exploration of coupled folding and binding of an intrinsically disordered molecular recognition element in measles virus nucleoprotein. Proc Natl Acad Sci USA. 2013;110(40):E3743–E3752. - PMC - PubMed
1. 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
1. Granata D, Camilloni C, Vendruscolo M, Laio A. Characterization of the free-energy landscapes of proteins by NMR-guided metadynamics. Proc Natl Acad Sci USA. 2013;110(17):6817–6822. - PMC - PubMed