Three Dimensional Model Myoglobin Molecule Obtained by Kendrew (3 results)

London, Macmillian and Co., 1958. Royal8vo. Bound in a green full cloth with gilt lettering to spine. Volume 181, from January to June, 1958, of "Nature" offered. Binding tight and clean externally as well as internally. Pp. 662-666. [Entire volume: CXLII, (2), 1816 pp]. First edition of the important paper in which the first three-dimensional model of a protein was obtained, and which thus laid the foundation for all structural biology. Kendrew was furthermore one of the first to use a computer in analyzing the data produced by x-ray diffraction. For his essential discovery Kendrew was awarded the Nobel Prize in Chemistry in 1962. The discovery is widely regarded as being one the most important in the second half of the 20th century within biology and chemistry. "The first dramatic but hard-won success of the approach [in understanding molecules], the determination of the three-dimensional structure of a protein called myoglobin, was announced in 1958 [in the present paper]. The findings laid the foundation for the age of structure in biology: [.] the paper was the outcome of a truly Herculean task. (Garwin, A century of Nature: twenty-one discoveries that changed science and the world, 2003, Pp. 87-88).…

London, Macmillian and Co, 1958 & 1960. Roayl8vo. 2 volumes, bound in contemporary half cloth with gilt lettering to spines. Stamps to front free end-paper and first leaf of each issue. In "Nature", vol. 181 & 185, 1958 & 1960, entire volumes offered. A fine set. [Nature 181, 1958:] pp. 662-666. [Nature 185, 1960:] pp. 422-27. [Entire volumes. CXLII, (2), 936 pp" LXXV, (1), 952 pp.]. First appearance of both papers in which the first three-dimensional model of a protein was presented, essential knowledge for progress in curing human diseases, thus laid the foundation for all structural biology. Kendrew was furthermore one of the first to use a computer in analyzing the data produced by x-ray diffraction. For his essential discovery Kendrew was awarded the Nobel Prize in Chemistry in 1962. The discovery is widely regarded as being one the most important in the second half of the 20th century within biology and chemistry. "The first dramatic but hard-won success of the approach [in understanding molecules], the determination of the three-dimensional structure of a protein called myoglobin, was announced in 1958 [in the present paper]. The findings laid the foundation for the age of structure in biology: [.] the paper was the outcome of a truly Herculean task. (Garwin, A century of Nature: twenty-one discoveries that changed science and the world, 2003, Pp. 87-88). The papers they produced (both offered here) are "the outcome of a truly Herculean task. When the project began, there were no automated instruments or digital computers for generating or analyzing the huge amounts of data necessary. Every step had to be carried out by hand. many repeated thousands of times" (A Century of Nature, p. 89) ?After the war, John Kendrew, a physical chemist who had occupied high offices in operational research during the war and, while on a common mission in Ceylon, had been convinced by Bernal of the promises of protein crystallography, joined Perutz to do a PhD. (Although working closely with Perutz, Kendrew was officially supervised by William T. Taylor, head of the crystallography division at the Cavendish" like most professional crystallographers Taylor regarded protein crystallography as a hopeless undertaking, but still accepted the formal agreement.) Kendrew first embarked on a comparative analysis of fetal and adult hemoglobin, but later switched to the simpler protein myoglobin, the oxygen carrier in muscle.? (DSB) Perutz now managed to attach a heavy atom (mercury) to the hemoglobin molecule. From the difference produced in the diffraction pattern he was able to deduce the phase of the reflections. The method had been known since the 1930s, but it had only been used for small molecules. Although the suggestion to apply the method to proteins dated from the same period, its applicability had not been proved. ?The problem consisted, firstly, in finding a heavy metal compound that could be attached to a specific site without altering the arrangement of the other atoms in the molecule and, secondly, in estimating with sufficient accuracy the overall changes in intensity produced by the heavy atoms. In Bragg?s judgment, Perutz?s skill in this last respect was ?probably unique? at the time (Bragg, 1965, p. 12). To this day, the isomorphous replacement method is considered the key method to determine the crystal structure of proteins. Kendrew, working on the smaller myoglobin molecule, was the first to take full advantage of the new method. In 1958, he presented the first model ever of a globular protein derived by direct structure determination. The model showed the general outline of the molecule a second model at atomic resolution followed two years later. In the same year Perutz presented the first model of hemoglobin at 5.5 Ångstrøm. Its four subunits proved to be closely related to the myoglobin molecule. The white-and-black disk model built of thermosetting plastic is still widely reproduced.? (DSB) The determination of any of these protein structures could not have been contemplated without the use of ever more powerful electronic computers. Perutz initially distrusted the new calculating devices and resisted resorting to the experimental digital computers developed at the nearby Mathematical Laboratory. Eventually he came around to recognize their usefulness, but he freely admitted that he was always hopeless at computing. He never made use of the machine himself and rather left this part of the work to the younger people in his group. Perutz and Kendrew shared the 1962 Nobel Prize for Chemistry for their work on the structure of proteins.? (DSB) Garrison & Morton: 6911 & 6912. …

1st Edition. Two volume first edition of a milestone in the history of structural biology, the first protein structure ever discovered. Kendrew's papers present the first solution of the three-dimensional molecular structure of a protein. "Kendrew's discovery was one of the greatest landmarks in the history of molecular biology" (Jeremy Norman History of Science). Along with his colleague Max Perutz, Kendrew received the 1952 Nobel Prize for this work. Two discoveries laid the foundation for Kendrew's work: "first, that the positions of atoms in a crystallized substance could be determined from X-rays passing through, and scattered by, the crystal; second, that the approach could be applied to very simple biological molecules (Garwin, Century of Nature, 88). The goal of Kendrew's team, composed mostly of physicists, was to understand how a biological molecule such as a protein works, beginning with how it is built. The papers they produced (both offered here) are "the outcome of a truly Herculean task. When the project began, there were no automated instruments or digital computers for generating or analyzing the huge amounts of data necessary. Every step had to be carried out by hand. many repeated thousands of times" (ibid, 89). Kendrew selected myoblobin as a protein because it abundant in the tissue in which it operated, is an oxygen-binding protein from muscle, and is very stable. His next step "was to measure the amplitudes of the 'reflections' - the scattered X-ray beams - produced when the crystals were exposed to X-radiation. Following this, he add up the measured reflections, in a process called Fourier summation, to produce an image of the molecules in the crystal lattice. "Photographic film was used to record the reflection amplitudes, thousands of them, and then teams. were trained to estimate their values by comparison with a known scale. The process took years. "The final step was the Fourier summation itself. Kendrew. [carried] out an earlier trial at lower resolution [and did] the summation by hand. For the more than 10,000 reflections that had to be added up at 2 angstrom resolution, hand summation was impossible. Technology came to the rescue: the first high-resolution protein structure ever determined was calculated on the first electronic computer ever built in Britain. "The resulting electron-density map looked impossible to interpret, [but] an ingenious system was devised for building the atomic model of the protein: the map was produced as a set of contoured topographic plots on sections through the crystal lattice; a three-dimensional grid was overlaid onto the map so that atomic coordinates could be measured with respect to three axes, x, y, and z, at right angles to each other; and wire rods were constructed whose height was proportional to the z-coordinate of each feature of density. Brass models were fabricated for each amino acid in the protein, and these were fitted by hand into the 'forest' of wires and secured by clamps" (ibid 90). The structure that resulted was not one anyone was prepared for - "the seeming irregularity of the overall polymer fold and the remarkable fact that the heme iron atom where oxygen bound was buried completely inside the protein" - and yet there were striking patterns, including the polymer chain folded into a series of eight segments (ibid). "After almost one hundred years of speculation, one could now see what a protein looked like in atomic detail" (ibid). CONDITION & DETAILS: 4to. (10.25 x 7.5 inches; 256 x 188mm). Ex-libris: bearing only a small circular stamp on the rear of the title page. Handsomely rebound in half calf over the original cloth covered boards. 5 raised bands at the spine, each gilt-ruled. Red and black morocco spine label, gilt-lettered. Tightly and very solidly bound. Bright and very clean throughout. Very good to near fine condition.…