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Structural ensembles of intrinsically disordered proteins depend strongly on force field: A comparison to experiment.

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Rauscher,  S.
Department of Theoretical and Computational Biophysics, MPI for Biophysical Chemistry, Max Planck Society;

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Gapsys,  V.
Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Gajda,  M. J.
Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society;

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Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society;

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de Groot,  B. L.
Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Grubmüller,  H.
Department of Theoretical and Computational Biophysics, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Rauscher, S., Gapsys, V., Zhou, M., Van, Q., Gajda, M. J., Zweckstetter, M., et al. (2016). Structural ensembles of intrinsically disordered proteins depend strongly on force field: A comparison to experiment. Biophysical Journal, 110(Suppl 1), 358A-358A.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002A-C15C-E
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