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Photo Marie Skepö

Marie Skepö

Professor

Photo Marie Skepö

Temperature Dependence of Intrinsically Disordered Proteins in Simulations : What are We Missing?

Author

  • S. Jephthah
  • L. Staby
  • B. B. Kragelund
  • M. Skepö

Summary, in English

The temperature dependence of the conformational properties in simulations of the intrinsically disordered model protein histatin 5 has been investigated using different combinations of force fields, water models, and atomistic and coarse-grained methods. The results have been compared to experimental data obtained from NMR, SAXS, and CD experiments to assess the accuracy and validity of the simulations. The results showed that neither simulations completely agreed with the experimental data, nor did they agree with each other. It was however possible to conclude that the observed conformational changes upon variations in temperature were not at all driven by electrostatic interactions. The final conclusion was that none of the simulations that were investigated in this study was able to accurately capture the temperature induced conformational changes of our model IDP.

Department/s

  • Computational Chemistry
  • eSSENCE: The e-Science Collaboration

Publishing year

2019

Language

English

Pages

2672-2683

Publication/Series

Journal of Chemical Theory and Computation

Volume

15

Issue

4

Document type

Journal article

Publisher

The American Chemical Society (ACS)

Topic

  • Theoretical Chemistry (including Computational Chemistry)

Status

Published

ISBN/ISSN/Other

  • ISSN: 1549-9618