We are writing to respond to the comment by Gapsys and de Groot, 2019 on our article about molecular dynamics simulations of human hemoglobin (El Hage et al., 2018).
The structure of the trypanosome haptoglobin-haemoglobin receptor bound to its ligand reveals the molecular basis for ligand recognition in innate immunity and identifies molecular determinants that aid efficient uptake.
Simulations of the unliganded human hemoglobin tetramer, which for the first time yield a thermodynamically stable system, cast doubts on the use of standard solvent box sizes for molecular dynamics studies of biological macromolecules.
Hemoglobin affinity and cooperativity reveal mechanistic insights in how the relation between physiology and evolutionary variations shape a protein's molecular property.
Multiple respiratory and vascular mechanisms have recurrently evolved across the vertebrates to alleviate the oxygen diffusion limitations inherent to the morphology of the retina.
The association of atypical memory B-cells and autoimmune antibodies (anti-phosphatidylserine) with hemoglobin levels in malaria patients uncovers a novel mechanism for the human malaria-induced anemia previously identified in mice.
A simulation study is used to demonstrate how mistakes in identifying the experimental unit and the unit of analysis can lead to incorrect analyses and inappropriate inferences when reporting research studies.
An international effort is needed to overcome the paywalls, customs regulations and lack of local suppliers that hinder research in low- and middle-income countries.
