Max F. Perutz
Affiliations: | MRC Laboratory of Molecular Biology, Cambridge, England, United Kingdom |
Area:
proteinsWebsite:
http://nobelprize.org/chemistry/laureates/1962/perutz-bio.htmlGoogle:
"Max F. Perutz"Bio:
(1914 - 2002)
http://www.nasonline.org/member-directory/deceased-members/45945.html
http://www.academia.edu/download/6422828/10.1.1.130.3814.pdf
DOI: 10.1038/143731b0
DOI: 10.1038/141523a0
The Nobel Prize in Chemistry 1962 was awarded jointly to Max Ferdinand Perutz and John Cowdery Kendrew "for their studies of the structures of globular proteins"
Mean distance: 7.59 (cluster 12) | S | N | B | C | P |
Cross-listing: Crystallography Tree - StructuralBiologyTree
Parents
Sign in to add mentorHerman F. Mark | research assistant | 1936 | Universität Wien |
John Desmond Bernal | grad student | 1940 | Cambridge |
W. Lawrence Bragg | post-doc | 1939-1947 | Cambridge (Physics Tree) |
Children
Sign in to add traineeJohn Kilmartin | grad student | Cambridge (Plant Biology Tree) | |
Noboru H. Komiyama | grad student | Wellcome Trust Sanger Institute (Neurotree) | |
Ben Luisi | grad student | MRC LMB | |
Francis Harry Compton Crick | grad student | 1954 | Cambridge |
David M. Blow | grad student | 1957 | Cambridge |
Hilary Muirhead | grad student | 1958 | Cambridge |
Keith Moffat | grad student | 1970 | Cambridge |
Howard Dintzis | post-doc | 1954-1956 | Cambridge |
Philip W. Tucker | post-doc | 1975-1977 | MRC-LMB (Cell Biology Tree) |
Michael G. Rossmann | research scientist | 1958-1964 | MRC-LMB |
Collaborators
Sign in to add collaboratorJohn C. Kendrew | collaborator | Cambridge | |
Hermann Lehmann | collaborator | MRC-LMB (GenetiTree) |
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Publications
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Perutz MF, Finch JT, Berriman J, et al. (2002) Amyloid fibers are water-filled nanotubes. Proceedings of the National Academy of Sciences of the United States of America. 99: 5591-5 |
Perutz M. (2000) Paul Sigler (1934-2000) Cell. 101: 23-24 |
Chen YW, Stott K, Perutz MF. (1999) Crystal structure of a dimeric chymotrypsin inhibitor 2 mutant containing an inserted glutamine repeat. Proceedings of the National Academy of Sciences of the United States of America. 96: 1257-61 |
Bettati S, Mozzarelli A, Perutz MF. (1998) Allosteric mechanism of haemoglobin: rupture of salt-bridges raises the oxygen affinity of the T-structure. Journal of Molecular Biology. 281: 581-5 |
Perutz MF, Wilkinson AJ, Paoli M, et al. (1998) The stereochemical mechanism of the cooperative effects in hemoglobin revisited. Annual Review of Biophysics and Biomolecular Structure. 27: 1-34 |
Perutz MF. (1995) Polar zippers: their role in human disease. Pharmaceutica Acta Helvetiae. 69: 213-24 |
Perutz MF, Shih DT, Williamson D. (1994) The chloride effect in human haemoglobin. A new kind of allosteric mechanism. Journal of Molecular Biology. 239: 555-60 |
Shih DT, Luisi BF, Miyazaki G, et al. (1993) A mutagenic study of the allosteric linkage of His(HC3)146 beta in haemoglobin. Journal of Molecular Biology. 230: 1291-6 |
Perutz MF, Fermi G, Poyart C, et al. (1993) A novel allosteric mechanism in haemoglobin. Structure of bovine deoxyhaemoglobin, absence of specific chloride-binding sites and origin of the chloride-linked Bohr effect in bovine and human haemoglobin. Journal of Molecular Biology. 233: 536-45 |
Camardella L, Caruso C, D'Avino R, et al. (1992) Haemoglobin of the antarctic fish Pagothenia bernacchii. Amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative. Journal of Molecular Biology. 224: 449-60 |