Nobel Prizes for 3D Molecular Structure: Difference between revisions
Eric Martz (talk | contribs) →Nobel Prizes for 3D Macromolecular Structure and Structure Determination Methods: adding myoglobin in jmol |
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<table align='right' width='300' border='0' cellpadding='10' bgcolor='#d0d0d0' hspace='8'><tr><td rowspan='2'> </td><td bgcolor='#e8e8e8' valign='top'> | <table align='right' width='300' border='0' cellpadding='10' bgcolor='#d0d0d0' hspace='8'><tr><td rowspan='2'> </td><td bgcolor='#e8e8e8' valign='top'> | ||
[[Image:Myoglobin1958.png]]</td><td bgcolor='#e8e8e8'><applet load=' | [[Image:Myoglobin1958.png]]</td><td bgcolor='#e8e8e8'><applet load='1mbn' size='160' frame='false' scene='Nobel_Prizes_for_3D_Molecular_Structure/1mbn/1' /></td></tr><tr><td bgcolor='#e8e8e8'>The first 3D protein structure: myoglobin at ~6 Å by Kendrew ''et al.''. Adapted by permission from Macmillan Publishers Ltd: Nature 181:662, copyright 1958.</td><td bgcolor='#e8e8e8'>Myoglobin ([[1mbn]], 2.0 Å) deposited in the fledgling [[PDB]] in 1973 by Watson and Kendrew.</td></tr></table> | ||
* 1962: [http://nobelprize.org/nobel_prizes/chemistry/laureates/1962/index.html Max Ferdinand Perutz and John Cowdery Kendrew] (Chemistry) "for their studies of the structures of globular proteins". With his coworkers, Kendrew obtained the first tertiary structure of a protein, myoglobin, in 1958 at about 6 Å [[resolution]]<ref name='kendrew58'>A three-dimensional model of the myoglobin molecule obtained by x-ray analysis. KENDREW JC, BODO G, DINTZIS HM, PARRISH RG, WYCKOFF H, PHILLIPS DC. Nature. 181:662-6, 1958. [http://www.ncbi.nlm.nih.gov/pubmed/13517261 PubMed 13517261]</ref>. Subsequently, they published higher resolution solutions for myoglobin. This achievement depended on the discovery, by Perutz and coworkers five years earlier, of heavy metal isomorphous replacement for phase determination in X-ray diffraction. In 1960, Perutz and coworkers solved oxy-hemoglobin at 5.5 Å resolution<ref>Structure of haemoglobin. A three-dimensional fourier syntheses at 5.5 Å resolution, obtained by X-ray analysis. M. F. Perutz, M. G. Rossman, A. F. Cullis, H. Muirhead, and G. Will. [http://www.nature.com/nature/journal/v185/n4711/pdf/185416a0.pdf Nature 185:416, 1960]. (Not in PubMed.)</ref>. The subsequent solution of deoxy hemoglobin by Muirhead and Perutz in 1962<ref>STRUCTURE OF HAEMOGLOBIN. A THREE-DIMENSIONAL FOURIER SYNTHESIS OF REDUCED HUMAN HAEMOGLOBIN AT 5-5 A RESOLUTION. MUIRHEAD H, PERUTZ MF. | * 1962: [http://nobelprize.org/nobel_prizes/chemistry/laureates/1962/index.html Max Ferdinand Perutz and John Cowdery Kendrew] (Chemistry) "for their studies of the structures of globular proteins". With his coworkers, Kendrew obtained the first tertiary structure of a protein, myoglobin, in 1958 at about 6 Å [[resolution]]<ref name='kendrew58'>A three-dimensional model of the myoglobin molecule obtained by x-ray analysis. KENDREW JC, BODO G, DINTZIS HM, PARRISH RG, WYCKOFF H, PHILLIPS DC. Nature. 181:662-6, 1958. [http://www.ncbi.nlm.nih.gov/pubmed/13517261 PubMed 13517261]</ref>. Subsequently, they published higher resolution solutions for myoglobin. This achievement depended on the discovery, by Perutz and coworkers five years earlier, of heavy metal isomorphous replacement for phase determination in X-ray diffraction. In 1960, Perutz and coworkers solved oxy-hemoglobin at 5.5 Å resolution<ref>Structure of haemoglobin. A three-dimensional fourier syntheses at 5.5 Å resolution, obtained by X-ray analysis. M. F. Perutz, M. G. Rossman, A. F. Cullis, H. Muirhead, and G. Will. [http://www.nature.com/nature/journal/v185/n4711/pdf/185416a0.pdf Nature 185:416, 1960]. (Not in PubMed.)</ref>. The subsequent solution of deoxy hemoglobin by Muirhead and Perutz in 1962<ref>STRUCTURE OF HAEMOGLOBIN. A THREE-DIMENSIONAL FOURIER SYNTHESIS OF REDUCED HUMAN HAEMOGLOBIN AT 5-5 A RESOLUTION. MUIRHEAD H, PERUTZ MF. | ||