HelenBerman01This image was used on the cover of the 2002 Annual Report of the Protein Data Bank (www.pdb.org)1 to honor Dr. Max Perutz.

Two horse hemoglobin structures (structures 2mhb2 and 2dhb3) are overlaid to show the conformational change that occurs when a ligand is bound to the heme group. The pioneering work of Dr. Max Perutz in X-ray crystallography of proteins won him the Nobel Prize in 1962. His life-long work on the allosteric mechanism for the cooperative binding of oxygen to hemoglobin won him respect throughout the scientific community.

  1. Berman, H.M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T.N., Weissig, H., Shindyalov, I.N., Bourne, P.E. (2000). The Protein Data Bank. Nucleic Acids Res. 28, 235-42.
  2. Ladner, R. C., Heidner, E. J. & Perutz, M. F. (1977). The structure of horse methaemoglobin at 2-0 A resolution. J Mol Biol 114(3), 385-414.
  3. Bolton, W. & Perutz, M. F. (1970). Three dimensional fourier synthesis of horse deoxyhaemoglobin at 2.8 Angstrom units resolution. Nature 228(271), 551-2.

For more information, visit Dr. Helen Berman's profile or the Protein Data Bank.

Year of Research Highlight: 2000