What is the true structure of liganded haemoglobin?
Does the crystal structure of a protein accurately represent its structure in solution? Or does the crystallization process perturb the structure significantly? Although aware of the problem, most crystallographers would argue that the highly solvated and weakly held lattice in protein crystals is, in general, unlikely to shift ordered parts of the molecule. In the case of conformationally flexible proteins, however, there is the possibility that one form might be favoured over another. Several lines of evidence suggest that this might be the case for the crystal structure of liganded Hb, although conflicting data exist.
Tame
J R
JR
Dept of Chemistry, University of York, Heslington, York, UK Y010 5DD.
D000818:Animals; D018360:Crystallography, X-Ray; D006454:Hemoglobins / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008024:Ligands; D011487:Protein Conformation
D006454:Hemoglobins; D008024:Ligands