Interpretation of interfacial protein spectra with enhanced molecular 
simulation ensembles.

Lutz, H.; Jaeger, V.; Weidner, T.; de Groot, B. L.

doi:10.1021/acs.jctc.8b00840

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Interpretation of interfacial protein spectra with enhanced molecular simulation ensembles.

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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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Citation

Lutz, H., Jaeger, V., Weidner, T., & de Groot, B. L. (2019). Interpretation of interfacial protein spectra with enhanced molecular simulation ensembles. Journal of Chemical Theory and Computation, 15(1), 698-707. doi:10.1021/acs.jctc.8b00840.

Cite as: https://hdl.handle.net/21.11116/0000-0002-A423-D

Abstract

An atomistically detailed picture of protein folding at interfaces can effectively be obtained by comparing interface-sensitive spectroscopic techniques to molecular simulations. Here, we present an extensive evaluation of the capability of contemporary force fields to model protein folding at air-water interfaces with a general scheme for sampling and reweighting theoretical conformational ensembles of interfacial peptides. Force field combinations of CHARMM22* / TIP3P and AMBER99SB*-ILDN / SPC/E were found to reproduce experimental observations best.