Cyrus Chothia

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Cyrus Chothia
Born Cyrus Homi Chothia
(1942-02-19) February 19, 1942 (age 72)[1]
Institutions
Alma mater University College London
Thesis The crystal structures of some molecules active at cholinergic nerve receptors (1973)
Doctoral advisor Peter J. Pauling[2]
Doctoral students
Other notable students Arthur Lesk (postdoc)
Notable awards
Website
www2.mrc-lmb.cam.ac.uk/group-leaders/emeritus/cyrus-chothia

Cyrus Homi Chothia (b. 19 Feb. 1942)[1] FRS is an emeritus scientist at the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB)[10][11] and emeritus fellow of Wolfson College, Cambridge.[8][12][13][14][15]

Education[edit]

Chothia was educated at Alleyn's School, then went to study at the Durham University graduating with a Bachelor of Science degree in 1965.[1] Chothia then completed a Master of Science degree at Birkbeck College in 1967 and a PhD in from University College London[9] under the supervision of Peter Pauling,[16] the son of Linus Pauling.

Research[edit]

After his Ph.D. Chothia worked in the Laboratory of Molecular Biology (LMB) for three years. He then worked with Michael Levitt at the Weizmann Institute of Science [17][18] followed by two years with Joel Janin at the Institut Pasteur in Paris.[19]

In 1976 Chothia returned to England to work at University College London and the LMB. With Arthur Lesk[20][21] he showed that proteins adapt to mutations by changes in structure.

In 1992 he proposed that most proteins are built of domains that come from a small number of families.[22] He collaborated with Alexey Murzin, Steven Brenner and Tim Hubbard to create the Structural Classification of Proteins (SCOP) database,[23][24] a periodic table for all known protein structures. With Julian Gough[5] to create the SUPERFAMILY database[25] which uses Hidden Markov models to identify protein sequences that are related to those of known structures.

Awards[edit]

Chothia was elected a Fellow of the Royal Society in 2000.[1] His candidacy reads:

References[edit]

  1. ^ a b c d "CHOTHIA, Cyrus Homi". Who's Who 2014. Who's Who (online Oxford University Press ed.). A & C Black an imprint of Bloomsbury Publishing plc.  (subscription required)
  2. ^ a b Cyrus Chothia at the Mathematics Genealogy Project
  3. ^ Gerstein, M.; Chothia, C. (1991). "Analysis of protein loop closure. Two types of hinges produce one motion in lactate dehydrogenase". Journal of Molecular Biology 220 (1): 133–149. doi:10.1016/0022-2836(91)90387-L. PMID 2067013.  edit
  4. ^ Gough, Julian John Thurstan (2002). Hidden Markov models and their application to genome analysis in the context of protein structure (PhD thesis). University of Cambridge. 
  5. ^ a b "Dr. Julian Gough's home page at the University of Bristol". Archived from the original on 2012-02-25. 
  6. ^ Bateman, Alexander George (1997). Evolution of the structure and function of the immunoglobulin superfamily (DPhil thesis). University of Cambridge. 
  7. ^ "Dr Alex Bateman - Wellcome Trust Sanger Institute". Archived from the original on 2012-02-25. 
  8. ^ a b "Wolfson College: Emeritus Fellow Dr Cyrus Chothia MA MSc FRS". Archived from the original on 2012-02-25. 
  9. ^ a b Chothia, Cyrus (1973). The crystal structures of some molecules active at cholinergic nerve receptors (PhD thesis). University College London. 
  10. ^ "Cyrus Chothia: The protein origins of biological complexity, LMB Emeritus". Archived from the original on 2012-02-25. 
  11. ^ "Structural genomics and protein structure". Mrc-lmb.cam.ac.uk. Retrieved 2014-06-24. 
  12. ^ "Cyrus Chothia profile on BiomedExperts". Biomedexperts.com. Retrieved 2014-06-24. 
  13. ^ List of publications from the DBLP Bibliography Server
  14. ^ "cyrus chothia - Google Scholar". Scholar.google.com. Retrieved 2014-06-24. 
  15. ^ Chothia, C.; Lesk, A. M.; Tramontano, A.; Levitt, M.; Smith-Gill, S. J.; Air, G.; Sheriff, S.; Padlan, E. A.; Davies, D.; Tulip, W. R.; Colman, P. M.; Spinelli, S.; Alzari, P. M.; Poljak, R. J. (1989). "Conformations of immunoglobulin hypervariable regions". Nature 342 (6252): 877–883. Bibcode:1989Natur.342..877C. doi:10.1038/342877a0. PMID 2687698. 
  16. ^ Chothia, C.; Pauling, P. (1969). "On the conformations of hallucinogenic molecules and their correlation". Proceedings of the National Academy of Sciences of the United States of America 63 (4): 1063–1070. doi:10.1073/pnas.63.4.1063. PMC 223427. PMID 4311249. 
  17. ^ Chothia, C.; Levitt, M.; Richardson, D. (1977). "Structure of proteins: Packing of alpha-helices and pleated sheets". Proceedings of the National Academy of Sciences of the United States of America 74 (10): 4130–4134. doi:10.1073/pnas.74.10.4130. PMC 431889. PMID 270659.  edit
  18. ^ Levitt, M.; Chothia, C. (1976). "Structural patterns in globular proteins". Nature 261 (5561): 552–558. Bibcode:1976Natur.261..552L. doi:10.1038/261552a0. PMID 934293.  edit
  19. ^ Sweet, R.; Wright, H.; Janin, J.; Chothia, C.; Blow, D. (1974). "Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6-A resolution". Biochemistry 13 (20): 4212–4228. doi:10.1021/bi00717a024. PMID 4472048. 
  20. ^ Lesk, A.; Chothia, C. (1980). "How different amino acid sequences determine similar protein structures: The structure and evolutionary dynamics of the globins". Journal of Molecular Biology 136 (3): 225–270. doi:10.1016/0022-2836(80)90373-3. PMID 7373651. 
  21. ^ Lesk, A.; Chothia, C. (1980). "Solvent accessibility, protein surfaces, and protein folding". Biophysical Journal 32 (1): 35–47. Bibcode:1980BpJ....32...35L. doi:10.1016/S0006-3495(80)84914-9. PMC 1327253. PMID 7248454. 
  22. ^ Chothia, C. (1992). "One thousand families for the molecular biologist". Nature 357 (6379): 543–4. doi:10.1038/357543a0. PMID 1608464. 
  23. ^ Hubbard, T.; Murzin, A.; Brenner, S.; Chothia, C. (1997). "SCOP: A structural classification of proteins database". Nucleic Acids Research 25 (1): 236–239. doi:10.1093/nar/25.1.236. PMC 146380. PMID 9016544.  edit
  24. ^ UK government grants awarded to Cyrus Chothia, Research Councils UK
  25. ^ Gough, J.; Chothia, C. (2002). "SUPERFAMILY: HMMs representing all proteins of known structure. SCOP sequence searches, alignments and genome assignments". Nucleic Acids Research 30 (1): 268–272. doi:10.1093/nar/30.1.268. PMC 99153. PMID 11752312. 
  26. ^ "Library and Archive Catalogue". London: The Royal Society. Retrieved 2013-11-18.