What is it about?
As you increase the temperature chemical reactions take place at a faster rate. This means that for every ten degrees the rate will usually double. In this study protein unfolding rates are modelled using molecular dynamics and rates do roughly double for every 10 degree temperature increase.
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Why is it important?
It is difficult to relate molecular dynamics simulations to calculated physical properties. By showing that the Arrhenius equation applies this paper supports the view that simulations are realistic and capture real-world properties. This study can be extended to compare the unfolding energies between different protein mutations. This is important for understanding protein stability.
Perspectives
There are a lot of publications that try to predict thermodynamic properties from molecular dynamics. A lot of them use a "correction" term to bring the simulation and experimental results together. The problem with this approach is that these corrections are often post-hoc and arbitrary. This leads to problems of reproducibility. If molecular dynamics is going to be used for predictions with solid foundations then it has to be statistically sound and also realistic. It needs to capture the physics of reality. This paper shows that to some degree the modelled systems do but there is still a long way to go in order to produce reliable calculations.
Dr Andrew R Dalby
University of Westminster
Read the Original
This page is a summary of: Molecular Dynamics Simulations of the Temperature Induced Unfolding of Crambin Follow the Arrhenius Equation., F1000Research, August 2015, Faculty of 1000, Ltd.,
DOI: 10.12688/f1000research.6831.1.
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