Temperature Dependence of Intrinsically Disordered Proteins in Simulations : What are We Missing?
(2019) In Journal of Chemical Theory and Computation 15(4). p.2672-2683- Abstract
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... (More)
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.
(Less)
- author
- Jephthah, S. LU ; Staby, L. ; Kragelund, B. B. and Skepö, M. LU
- organization
- publishing date
- 2019
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Chemical Theory and Computation
- volume
- 15
- issue
- 4
- pages
- 12 pages
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- scopus:85064174559
- pmid:30865820
- ISSN
- 1549-9618
- DOI
- 10.1021/acs.jctc.8b01281
- language
- English
- LU publication?
- yes
- id
- 7b6ef2b5-4db4-4187-b7bd-ba58127f1d2a
- date added to LUP
- 2019-04-25 08:57:00
- date last changed
- 2024-06-11 08:58:57
@article{7b6ef2b5-4db4-4187-b7bd-ba58127f1d2a,
abstract = {{<p>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.</p>}},
author = {{Jephthah, S. and Staby, L. and Kragelund, B. B. and Skepö, M.}},
issn = {{1549-9618}},
language = {{eng}},
number = {{4}},
pages = {{2672--2683}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Journal of Chemical Theory and Computation}},
title = {{Temperature Dependence of Intrinsically Disordered Proteins in Simulations : What are We Missing?}},
url = {{http://dx.doi.org/10.1021/acs.jctc.8b01281}},
doi = {{10.1021/acs.jctc.8b01281}},
volume = {{15}},
year = {{2019}},
}