|Born||Cyrus Homi Chothia
February 19, 1942 
|Alma mater||University College London|
|Thesis||The crystal structures of some molecules active at cholinergic nerve receptors (1973)|
|Doctoral advisor||Peter J. Pauling|
|Other notable students||Arthur Lesk (postdoc)|
Cyrus Homi Chothia (b. 19 Feb. 1942) FRS is an emeritus scientist at the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) and emeritus fellow of Wolfson College, Cambridge.
Chothia was educated at Alleyn's School, then went to study at the Durham University graduating with a Bachelor of Science degree in 1965. Chothia then completed a Master of Science degree at Birkbeck College in 1967 and a PhD in from University College London under the supervision of Peter Pauling, the son of Linus Pauling.
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  followed by two years with Joel Janin at the Institut Pasteur in Paris.
In 1992 he proposed that most proteins are built of domains that come from a small number of families. He collaborated with Alexey Murzin, Steven Brenner and Tim Hubbard to create the Structural Classification of Proteins (SCOP) database, a periodic table for all known protein structures. With Julian Gough to create the SUPERFAMILY database which uses Hidden Markov models to identify protein sequences that are related to those of known structures.
|“||Dr Chothia has shown how the amino sequences of proteins determine their structure, function and evolution. From an analysis of their structural regularities, he has developed a classification of protein structures that is now in general use. His picture of protein evolution suggests how proteins diverge and gain new functions. He has helped us to understand how their apparently limited set of slightly different structures allow immunoglobin to recognise an almost limitless variety of different antigens.||”|
- CHOTHIA, Cyrus Homi. Who's Who 2014 (online Oxford University Press ed.). A & C Black an imprint of Bloomsbury Publishing plc. (subscription required)
- Cyrus Chothia at the Mathematics Genealogy Project
- 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.
- 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.
- "Dr. Julian Gough's home page at the University of Bristol". Archived from the original on 2012-02-25.
- Bateman, Alexander George (1997). Evolution of the structure and function of the immunoglobulin superfamily (DPhil thesis). University of Cambridge.
- "Dr Alex Bateman - Wellcome Trust Sanger Institute". Archived from the original on 2012-02-25.
- "Wolfson College: Emeritus Fellow Dr Cyrus Chothia MA MSc FRS". Archived from the original on 2012-02-25.
- Chothia, Cyrus (1973). The crystal structures of some molecules active at cholinergic nerve receptors (PhD thesis). University College London.
- "Cyrus Chothia: The protein origins of biological complexity, LMB Emeritus". Archived from the original on 2012-02-25.
- "Structural genomics and protein structure". Mrc-lmb.cam.ac.uk. Retrieved 2014-06-24.
- "Cyrus Chothia profile on BiomedExperts". Biomedexperts.com. Retrieved 2014-06-24.
- List of publications from the DBLP Bibliography Server
- "cyrus chothia - Google Scholar". Scholar.google.com. Retrieved 2014-06-24.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- Chothia, C. (1992). "One thousand families for the molecular biologist". Nature 357 (6379): 543–4. doi:10.1038/357543a0. PMID 1608464.
- 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.
- UK government grants awarded to Cyrus Chothia, Research Councils UK
- 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.
- "Library and Archive Catalogue". London: The Royal Society. Retrieved 2013-11-18.