Max F. Perutz

Affiliations: 
MRC Laboratory of Molecular Biology, Cambridge, England, United Kingdom 
Area:
proteins
Website:
http://nobelprize.org/chemistry/laureates/1962/perutz-bio.html
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"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)
 
SNBCP
Cross-listing: Crystallography Tree - StructuralBiologyTree

Parents

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Herman 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

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John 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
Michael G. Rossmann research scientist 1958-1964 MRC-LMB

Collaborators

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John C. Kendrew collaborator Cambridge
Hermann Lehmann collaborator MRC-LMB (GenetiTree)
BETA: Related publications

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
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
Fermi G, Perutz MF, Williamson D, et al. (1992) Structure-function relationships in the low-affinity mutant haemoglobin Aalborg (Gly74 (E18)beta----Arg). Journal of Molecular Biology. 226: 883-8
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