X-ray crystallographic analyses of symmetrical allosteric effectors of hemoglobin: compounds designed to link primary and secondary binding sites

The rational design and X-ray crystallographic analyses of two symmetrical allosteric effectors of hemoglobin are reported. Both compounds were found to span and link primary and secondary allosteric sites.

Structure of human carbonmonoxyhemoglobin at 2.16 Å: a snapshot of the allosteric transition

A new structure of carbonmonoxyhemoglobin solved at 2.16 Å is reported. The new structure, obtained using a lower pH, shows significant strain at the α1β2 (α2β1) interface, suggests initiation of the R to T allosteric transition.