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Comment
. 2013 Apr 9;110(15):5744-5.
doi: 10.1073/pnas.1303539110. Epub 2013 Apr 1.

A "slow" protein folds quickly in the end

Affiliations
Comment

A "slow" protein folds quickly in the end

Robert B Best. Proc Natl Acad Sci U S A. .
No abstract available

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Conflict of interest statement

The author declares no conflict of interest.

Comment on

  • Atomic-level description of ubiquitin folding.
    Piana S, Lindorff-Larsen K, Shaw DE. Piana S, et al. Proc Natl Acad Sci U S A. 2013 Apr 9;110(15):5915-20. doi: 10.1073/pnas.1218321110. Epub 2013 Mar 15. Proc Natl Acad Sci U S A. 2013. PMID: 23503848 Free PMC article.

References

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    1. Lindorff-Larsen K, et al. Improved side-chain torsion potentials for the Amber ff99SB protein force field. Proteins. 2010;78(8):1950–1958. - PMC - PubMed
    1. Piana S, Lindorff-Larsen K, Shaw DE. How robust are protein folding simulations with respect to force field parameterization? Biophys J. 2011;100(9):L47–L49. - PMC - PubMed
    1. Best RB, Hummer G. Optimized molecular dynamics force fields applied to the helix-coil transition of polypeptides. J Phys Chem B. 2009;113(26):9004–9015. - PMC - PubMed
    1. Freddolino PL, Harrison CB, Liu Y, Schulten K. Challenges in protein folding simulations: Timescale, representation, and analysis. Nat Phys. 2010;6(10):751–758. - PMC - PubMed

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