Interpretation of Interfacial Protein Spectra with Enhanced Molecular Simulation Ensembles

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  • Helmut Lutz, Max-Planck Institute for Polymer Research, Mainz, Tyskland
  • Vance Jaeger, Max-Planck Institute for Biophysical Chemistry, Göttingen, Tyskland
  • Tobias Weidner
  • Bert L. de Groot, Max Planck Inst Biophys Chem, Max Planck Society, Dept Theoret & Computat Biophys, Max-Planck Institute for Biophysical Chemistry, Göttingen

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.

TidsskriftJournal of Chemical Theory and Computation
Sider (fra-til)698-707
Antal sider10
StatusUdgivet - 2019
Eksternt udgivetJa

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