Bioinformatics and Functional Genomics, Second Edition

Beginning in the 1940s, Max Perutz and John Kendrew realized the goal of determining the structure of globular proteins by solving the structure of hemoglobin and myoglobin. In recognition of this work, they shared the Nobel Prize in Chemistry in 1962. (top) X-ray precession photograph of a myoglobin crystal (from http://www.nobel.se/chemistry/laureates/1962/kendrew-lecture.pdf). Kendrew studied myoglobin from the sperm whale (Physeter catodon), and incorporated a heavy metal by the method of isomorphous replacement. He could then bombard the crystals with x-rays in order to obtain an x-ray diffraction pattern (such as that shown here) with which to deduce the electron density throughout the crystal. This required the analysis of 25,000 reflections. (middle) Perutz and Kendrew used the EDSAC I computer (introduced in 1949 and shown here (from http://www.cl.cam.ac.uk/Relics/jpegs/edsac99.36.jpg). This computer was essential to interpret the diffraction patterns. For a simulator that shows the capacity of the EDSAC machine, see http://www.dcs.warwick.ac.uk/~edsac/. (bottom) Photograph ...