1971: Structure and Function of Proteins at the Three-Dimensional Level, Vol. XXXVI
Organizer: James Watson
Reginald Harris had been established the Symposia in 1933 because he wanted to promote a quantitative approach to biological research that would require the skills of mathematicians, chemists and physicists, as well as biologists. In the early days of the Symposia, topics such as membrane permeability and nerve conduction had been at the cutting edge of biophysical research, but by 1971 X-ray crystallographic analysis of protein structure occupied center stage.
The science of protein X-ray crystallography had been established in 1934 when Bernal and Crowfoot had obtained the first diffraction pattern from a protein in 193. Major advances came rather slowly—Pauling and Corey had published their great series of papers—including descriptions of the alpha helix and beta sheets—in 1951 and Perutz demonstrated the power of isomorphous heavy atom replacement in 1953. The first protein structure—that of myoglobin—had been determined by Kendrew only in 1957, followed by Perutz analysis of hemoglobin in 1959.
But now the Symposium included papers describing structural analyses of chymotrypsin, elastase, subtilisin, and trypsin, to name just those proteins appearing in the session on proteases. Nor were the data restricted to structure determination pure and simple. There were papers describing the insights molecular structure was bringing to the mechanisms by which proteins carried out their work. Most notably, Max Perutz expanded on his comparative studies of hemoglobin and oxyhemoglobin and how these illuminated the Bohr Effect—that hemoglobin binds oxygen more readily
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at low pH and gives it up more readily at higher pHs.
The meeting was attended by many notable protein scientists, including Nobel Laureates Dorothy Hodgkin, Aaron Klug, William Lipscomb and Max Perutz. Sadly absent was William Lawrence Bragg, who with his father, had established the field of X-ray crystallography 59 years earlier. He had not been well and died shortly after the Symposium, on 1 July. The Symposium volume began with a tribute to him and David Phillips, in his closing summary, remarked that Bragg had been "...certain that we are still at the beginning of biological crystallography..." Brag was right and would have been astounded to learn that by 2002, the Protein Data Bank contained 17,902 structures, of which no fewer 4000 were added in 2001. And he would have been thrilled to see how X-ray crystallography is illuminating the functions of huge multimolecular complexes such as the ribosome (see Symposium , 2001)
— Jan A. Witkowski |
