Hemoglobin: Studying the T to R Transition

Hemoglobin, a tetrameric protein found in high concentrations in red blood cells, is responsible for binding and transporting oxygen in the body. Each hemoglobin protein is made up of four subunits - two alpha subunits and two beta subunits - and each subunit is capable of binding to an oxygen molecule via its heme group. This animated pathway shows conformational changes upon oxygen binding, focusing first on a heme group and then zooming out to see the structure of the tetramer and then shows conformation changes from T to R states, and finally allosteric regulation by BPG.

Topics

  • bisphosphoglycerate
  • BPG
  • allostery
  • allosteric effectors
  • hemoglobin T to R transition
  • hemoglobin
  • regulation
  • conformational changes
  • oxygen
  • oxygen binding
  • proteins
  • tetrameric protein
  • dimer
  • alpha-beta
  • alpha
  • beta