Nobel Prizes for 3D Molecular Structure: Difference between revisions
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* 1985: [http://nobelprize.org/nobel_prizes/chemistry/laureates/1985/index.html Herbert A. Hauptman and Jerome Karle] (Chemistry) "for their outstanding achievements in the development of '''direct''' methods for the determination of crystal structures". | * 1985: [http://nobelprize.org/nobel_prizes/chemistry/laureates/1985/index.html Herbert A. Hauptman and Jerome Karle] (Chemistry) "for their outstanding achievements in the development of '''direct''' methods for the determination of crystal structures". | ||
* 2011: [http://nobelprize.org/nobel_prizes/chemistry/laureates/2011/index.html Dan Shechtman] (Chemistry) "for the discovery of quasicrystals". | |||
* 2013: [https://www.nobelprize.org/prizes/chemistry/2013/summary Martin Karplus Michael Levitt & Arieh Warshel] "for the development of multiscale models for complex chemical systems" | |||
==Nobel Prizes for 3D Macromolecular Structure and Structure Determination Methods== | ==Nobel Prizes for 3D Macromolecular Structure and Structure Determination Methods== | ||
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* 1962 [http://nobelprize.org/nobel_prizes/medicine/laureates/1962/index.html Francis Harry Compton Crick, James Dewey Watson, and Maurice Hugh Frederick Wilkins] (Physiology or Medicine) "for their discoveries concerning the molecular structure of nucleic acids and its significance for information transfer in living material". Although Watson and Crick's 1953 model<ref>Molecular Structure of Nucleic Acids: A Structure for Deoxyribose Nucleic Acid. J. D. WATSON, F. H. C. CRICK, Nature 171, 737 - 738, 1953. [http://www.exploratorium.edu/origins/coldspring/ideas/printit.html Free annotated PDF from the Exploratorium].</ref> was theoretical, based in part on X-ray fiber diffraction, it was essentially correct, and for the first time explained the ability of genes to be faithfully copied during cell division. It was not confirmed by atomic resolution X-ray crystallography until 1973, using RNA dinucleotide crystals<ref name='berman'>Nucleic acid crystallography: a view from the nucleic acid database. Berman HM, Gelbin A, Westbrook J. Prog Biophys Mol Biol. 66:255-88, 1996. [http://www.ncbi.nlm.nih.gov/pubmed/9284453 PubMed 9284453]</ref>. A full turn of B form DNA was not solved until 1980 ([[1bna|1BNA]])<ref name='berman' />, 27 years after Watson and Crick's model. X-ray diffraction data obtained by [http://en.wikipedia.org/wiki/Rosalind_franklin Rosalind E. Franklin] (1920-1958) played an important role in Crick, Wilkins and Watson's model building, but she regrettably received inadequate credit in the 1953 publication<ref>Rosalind Franklin: Dark Lady of DNA by Brenda Maddox, HarperCollins, 2002</ref>. | * 1962 [http://nobelprize.org/nobel_prizes/medicine/laureates/1962/index.html Francis Harry Compton Crick, James Dewey Watson, and Maurice Hugh Frederick Wilkins] (Physiology or Medicine) "for their discoveries concerning the molecular structure of nucleic acids and its significance for information transfer in living material". Although Watson and Crick's 1953 model<ref>Molecular Structure of Nucleic Acids: A Structure for Deoxyribose Nucleic Acid. J. D. WATSON, F. H. C. CRICK, Nature 171, 737 - 738, 1953. [http://www.exploratorium.edu/origins/coldspring/ideas/printit.html Free annotated PDF from the Exploratorium].</ref> was theoretical, based in part on X-ray fiber diffraction, it was essentially correct, and for the first time explained the ability of genes to be faithfully copied during cell division. It was not confirmed by atomic resolution X-ray crystallography until 1973, using RNA dinucleotide crystals<ref name='berman'>Nucleic acid crystallography: a view from the nucleic acid database. Berman HM, Gelbin A, Westbrook J. Prog Biophys Mol Biol. 66:255-88, 1996. [http://www.ncbi.nlm.nih.gov/pubmed/9284453 PubMed 9284453]</ref>. A full turn of B form DNA was not solved until 1980 ([[1bna|1BNA]])<ref name='berman' />, 27 years after Watson and Crick's model. X-ray diffraction data obtained by [http://en.wikipedia.org/wiki/Rosalind_franklin Rosalind E. Franklin] (1920-1958) played an important role in Crick, Wilkins and Watson's model building, but she regrettably received inadequate credit in the 1953 publication<ref>Rosalind Franklin: Dark Lady of DNA by Brenda Maddox, HarperCollins, 2002</ref>. | ||
* 1972: [http://nobelprize.org/nobel_prizes/chemistry/laureates/1972/index.html Christian B. Anfinsen, Stanford Moore, and William H. Stein] (Chemistry). Anfinsen "for his work on ribonuclease, especially concerning the connection between the amino acid sequence and the biologically active conformation", and Moore and Stein "for their contribution to the understanding of the connection between chemical structure and catalytic activity of the active centre of the ribonuclease molecule". This prize was '''not for structure determination''', but rather, in part, for determining the amino acids essential to the active site of the enzyme before the structure was determined. The structure of ribonuclease was reported independently by two groups in 1967<ref name='earliest'>References and [[PDB codes]] will be found at [http://www.umass.edu/microbio/rasmol/1st_xtls.htm Earliest Solutions for Macromolecular Crystal Structures].</ref>. It was the second enzyme structure to be solved, after lysozyme<ref name='earliest' />, and did not earn a Nobel prize. | * 1972: [http://nobelprize.org/nobel_prizes/chemistry/laureates/1972/index.html Christian B. Anfinsen, Stanford Moore, and William H. Stein] (Chemistry). Anfinsen "for his work on ribonuclease, especially concerning the connection between the amino acid sequence and the biologically active conformation", and Moore and Stein "for their contribution to the understanding of the connection between chemical structure and catalytic activity of the active centre of the ribonuclease molecule". This prize was '''not for structure determination''', but rather, in part, for determining the amino acids essential to the active site of the enzyme before the structure was determined. See also [[RNaseA Nobel Prizes]]. The structure of ribonuclease was reported independently by two groups in 1967<ref name='earliest'>References and [[PDB codes]] will be found at [http://www.umass.edu/microbio/rasmol/1st_xtls.htm Earliest Solutions for Macromolecular Crystal Structures].</ref>. It was the second enzyme structure to be solved, after lysozyme<ref name='earliest' />, and did not earn a Nobel prize. | ||
* 1982: [http://nobelprize.org/nobel_prizes/chemistry/laureates/1982/index.html Aaron Klug] (Chemistry) "for his development of crystallographic electron microscopy and his structural elucidation of biologically important nucleic acid-protein complexes". Klug and coworkers elucidated the structure of Tobacco Mosaic Virus and chromatin. The [http://nobelprize.org/nobel_prizes/chemistry/laureates/1982/press.html Nobel press release] explains | * 1982: [http://nobelprize.org/nobel_prizes/chemistry/laureates/1982/index.html Aaron Klug] (Chemistry) "for his development of crystallographic electron microscopy and his structural elucidation of biologically important nucleic acid-protein complexes". Klug and coworkers elucidated the structure of Tobacco Mosaic Virus and chromatin. The [http://nobelprize.org/nobel_prizes/chemistry/laureates/1982/press.html Nobel press release] explains | ||
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===Twenty-First Century=== | ===Twenty-First Century=== | ||
====2000-2009==== | |||
* 2002: [http://nobelprize.org/nobel_prizes/chemistry/laureates/2002/index.html John B. Fenn, Koichi Tanaka, and Kurt Wüthrich] (Chemistry) "for the development of methods for identification and structure analyses of biological macromolecules". Fenn and Tanaka each were awarded one quarter of the prize "for their development of soft desorption ionisation methods for mass spectrometric analyses of biological macromolecules", while Wüthrich received his half "for his development of nuclear magnetic resonance spectroscopy for determining the three-dimensional structure of biological macromolecules in solution". | * 2002: [http://nobelprize.org/nobel_prizes/chemistry/laureates/2002/index.html John B. Fenn, Koichi Tanaka, and Kurt Wüthrich] (Chemistry) "for the development of methods for identification and structure analyses of biological macromolecules". Fenn and Tanaka each were awarded one quarter of the prize "for their development of soft desorption ionisation methods for mass spectrometric analyses of biological macromolecules", while Wüthrich received his half "for his development of nuclear magnetic resonance spectroscopy for determining the three-dimensional structure of biological macromolecules in solution". | ||
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* 2006: [http://nobelprize.org/nobel_prizes/chemistry/laureates/2006/index.html Roger Kornberg] (Chemistry) "for his studies of the molecular basis of eukaryotic transcription". Kornberg and his group solved the structure of DNA-dependent '''RNA polymerase'''. In 1959, Roger saw his father Arthur Kornberg receive the Nobel Prize in Physiology or Medicine, with Severo Ochoa, for discovering DNA polymerase and describing the mechanism of DNA replication. The first RNA polymerase structures, from early 2001: [[1i3q]], [[1i50]], [[1i6h]], followed by others. | * 2006: [http://nobelprize.org/nobel_prizes/chemistry/laureates/2006/index.html Roger Kornberg] (Chemistry) "for his studies of the molecular basis of eukaryotic transcription". Kornberg and his group solved the structure of DNA-dependent '''RNA polymerase'''. In 1959, Roger saw his father Arthur Kornberg receive the Nobel Prize in Physiology or Medicine, with Severo Ochoa, for discovering DNA polymerase and describing the mechanism of DNA replication. The first RNA polymerase structures, from early 2001: [[1i3q]], [[1i50]], [[1i6h]], followed by others. | ||
* 2009: [http://nobelprize.org/nobel_prizes/chemistry/laureates/2009/index.html Venkatraman Ramakrishnan, Thomas A. Steitz, and Ada E. Yonath] (Chemistry) "for studies of the structure and function of the ribosome". The structure of the ribosome, published in 2000, revealed that the peptidyl transferase is a ribozyme, rather than a protein enzyme, despite protein comprising 40-50% of ribosomal mass. A 2.4 Å structure of the large (50S) subunit from ''Haloarcula marismortui'', [[1ffk]], was published in ''Science'' by the Steitz group (Yale University, New Haven, CT, USA) in August, 2000. One month later appeared in ''Nature'' a 3.0 Å structure of the small (30S) subunit, [[1fjg]], from the Ramakrishnan group (MRC Laboratory of Molecular Biology, Cambridge, United Kingdom), and in ''Cell'' a 3.3 Å structure of the small subunit, [[1fka]], by the Yonath group (Weizmann Institute of Science, Rehovot, Israel). Less than a year later appeared in ''Science'' a 5.5 Å structure of the entire ribosome, [[1gix]] plus [[1giy]], from the group of Harry F. Noller (University of California, Santa Cruz). All were from ''Thermus thermophilus'', with the exception of the Steitz group's structure; all were from [[extremophiles]]. In subsequent years, these and other groups contributed many more highly informative structures (some are listed at [[Ribosome|the ribosome entry]]). | |||
** [http://www.pdb.org/pdb/static.do?p=general_information/news_publications/news/news_2009.html#20091013 Announcement at the RCSB PDB]. | |||
** [http://www.nigms.nih.gov/News/Results/nobel_20091007a.htm Three NIGMS Grantees Receive Nobel Prize in Chemistry for Ribosome Research]. | |||
** [[Ribosome|The Ribosome]] in Proteopedia. | |||
** [http://www.pdb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb10_1.html October 2000 Molecule of the Month]. | |||
** [[Highest_impact_structures|Highest Impact Structures of All Time]]. | |||
====2010-2019==== | |||
* 2012: [http://www.nobelprize.org/nobel_prizes/chemistry/laureates/2012/ Robert J. Lefkowitz and Brian K. Kobilka share the 2012 Nobel Prize in Chemistry] for work on [[G protein-coupled receptor |G protein-coupled receptors]] that includes solving the first structures of a ligand-activated G protein-coupled receptor ([[2r4r]], [[2r4s]], & [[2rh1]] in 2007) and the first activated G protein-coupled receptor in complex with its G protein ([[3sn6]] in 2011). | |||
** A detailed description of the laureates' body of work on this class of receptors with images is [http://www.nobelprize.org/nobel_prizes/chemistry/laureates/2012/popular-chemistryprize2012.pdf here]. | |||
** [[G protein-coupled receptor |G protein-coupled receptors]] in Proteopedia. | |||
* 2017: [https://www.nobelprize.org/prizes/chemistry/2017/summary/ Jacques Dubochet, Joachim Frank, and Richard Henderson share the 2017 Nobel Prize in Chemistry] "for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution." | |||
** [https://www.youtube.com/watch?v=026rzTXb1zw 5 min video] explaining their contributions. | |||
** Richard Henderson explains the history of cryo-EM in this [https://www.youtube.com/watch?v=L6U--sYUF9s 11 min video], and elaborates on single-particle cryo-EM in this [https://www.youtube.com/watch?v=j_sfs6uwWlc 14 min video]. | |||
====2020-2029==== | |||
* 2024: [https://www.nobelprize.org/prizes/chemistry/2024/summary/ David Baker, Demis Hassabis, and John M. Jumper share the 2024 Nobel Prize in Chemistry], Baker for "computational protein design", Hassabis and Jumper for "protein structure prediction" ([[AlphaFold]]). | |||
** [https://www.youtube.com/watch?v=cx7l9ZGFZkw 22 min video] explaining their contributions. | |||
** [https://www.youtube.com/watch?v=g96tXNwrYXc 9 min video] of David Baker explaining his protein design work. | |||
** [https://www.youtube.com/watch?v=SdxOouXsaxc 4 min video] of Demis Hassabis and John Jumper reacting to their Nobel Prize. | |||
** The [https://www.nobelprize.org/prizes/physics/2024/press-release/ 2024 Nobel Prize in Physics went to John J. Hopfield and Geoffrey E. Hinton] for machine learning with neural networks, technology that underlies the prizewinning work in Chemistry. | |||
==See Also== | ==See Also== | ||
*[[RNaseA Nobel Prizes]] | |||
*[http://nobelprize.org NobelPrize.Org]. | *[http://nobelprize.org NobelPrize.Org]. | ||
*[http://almaz.com/nobel/nobel.html Nobel Prize Internet Archive], a particularly useful set of lists because it includes the subjects of each prize next to the names of the prize winners. | *[http://almaz.com/nobel/nobel.html Nobel Prize Internet Archive], a particularly useful set of lists because it includes the subjects of each prize next to the names of the prize winners. | ||