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Journal Article

Secondary structure propensities in peptide folding simulations: A systematic comparison of molecular mechanics interaction schemes.

MPS-Authors
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Matthes,  D.
Research Group of Computational Biomolecular Dynamics, 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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588029.pdf
(Publisher version), 2MB

Supplementary Material (public)

588029_Suppl.pdf
(Supplementary material), 14MB

Citation

Matthes, D., & de Groot, B. L. (2009). Secondary structure propensities in peptide folding simulations: A systematic comparison of molecular mechanics interaction schemes. Biophysical Journal, 97(2), 599-608. Retrieved from http://download.cell.com/biophysj/pdf/PIIS0006349509009801.pdf.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0012-D7E0-7
Abstract
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