Heme Binding
This animation was created for an online module for the Scientific Foundations of Medicine course at the Johns Hopkins University School of Medicine. It was made in collaboration with Dr. Sandra Gabelli and Dr. Jon Lorch from the Department of Biophysics and Biophysical Chemistry at Johns Hopkins. The 3D models and animations were created in Cinema 4D and composited and further animated in After Effects.
Narration: Movement of the iron atom into the plane of the heme upon oxygen binding triggers the T to R conformational shift in the hemoglobin molecule. In deoxyhemoglobin, the iron atoms are about 0.6 angstroms out of the heme plane on the side of the proximal histidine residues; you can imagine that the histidines are pulling the iron atoms down and though this is not really accurate, it is a useful way to remember it.
In this 3D medical animation: Hemoglobin, Dimer, Monomer, Polypeptide chain, Iron atom, Oxygen, Molecule, Proximal histidine residue, Histidine