Comment on 'Valid molecular dynamics simulations of human hemoglobin require a surprisingly large box size'.
Level V
Where this comes from
- Record sourced from PubMed, PMID 31219782.
- Also identified by DOI 10.7554/eLife.44718 and PMC identifier 6586461.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
A recent molecular dynamics investigation into the stability of hemoglobin concluded that the unliganded protein is only stable in the T state when a solvent box is used in the simulations that is ten times larger than what is usually employed (El Hage et al., 2018). Here, we express three main concerns about that study. In addition, we find that with an order of magnitude more statistics, the reported box size dependence is not reproducible. Overall, no significant effects on the kinetics or thermodynamics of conformational transitions were observed.
Medical subject headings
- Hemoglobins
- Molecular Dynamics Simulation