Michael Levitt

Michael Levitt
Michael Levitt;
Michael Levitt
	Levitt during the Royal Swedish Academy of Sciences press conference in Stockholm in December 2013
Born	9 May 1947 (aged 79) ; Pretoria, South Africa
Citizenship	American; British; Israeli; South African;
Education	Pretoria Boys High School
Alma mater	King's College London (BScs); University of Cambridge (PhD)
Awards	EMBO Membership (1983); Member of the National Academy of Sciences (2002); Nobel Prize in Chemistry (2013); DeLano Award (2014); ISCB Fellow (2015);
	Scientific career
Fields	Computational Structural Biology; Structure Determination; Simulation of Mesoscale Molecular dynamics;
Institutions	Stanford University; Weizmann Institute of Science; Laboratory of Molecular Biology; University of Cambridge;
Thesis	Conformation analysis of proteins (1972)
Notable students	(postdocs); Steven Brenner[source?]; Cyrus Chothia; Valerie Daggett; Mark Gerstein; Julian Gough; Ram Samudrala;
Website	csb.stanford.edu/levitt; med.stanford.edu/profiles/Michael_Levitt

Michael Levitt, (Hebrew: מיכאל לויטcode: he is deprecated ; born 9 May 1947) is a South African biophysicist. He is a professor of structural biology at Stanford University, a position he has held since 1987.^[11]^[12] Levitt received the 2013 Nobel Prize in Chemistry.^[13]

References

↑ LEVITT, Prof. Michael. Who's Who. ukwhoswho.com 2003A & C Black, an imprint of Bloomsbury Publishing plc. (subscription needed)
↑ ^2.0 ^2.1 ^2.2 ^2.3 Siegel-Itzkovich, Judy (9 October 2013). "Two American Israelis and US jew share Nobel Prize in Chemistry". The Jerusalem Post. http://www.jpost.com/Jewish-World/Jewish-Features/Israeli-scientists-awarded-Nobel-Prize-in-Chemistry-328246. Retrieved 12 November 2017.
↑ Anon. Michael Levitt EMBO profile. people.embo.org (1983). Heidelberg: European Molecular Biology Organization.
↑ Anon. ISCB Fellows. iscb.org (2017)International Society for Computational Biology.
↑ Levitt, M.. The birth of computational structural biology. Nature Structural Biology 8 (5) (2001). p. 392–393. doi:10.1038/87545.
↑ Diamond, R.. A refinement of the structure of lysozyme. Biochemical Journal 125 (4) (1971). p. 92P. doi:10.1042/bj1250092Pa.
↑ Daggett, V.. Protein Unfolding Pathways Explored Through Molecular Dynamics Simulations. Journal of Molecular Biology 232 (2) (1993). p. 600–619. doi:10.1006/jmbi.1993.1414.
↑ Gerstein, M.. A structural census of the current population of protein sequences. PNAS 94 (22) (1997). p. 11911–11916. doi:10.1073/pnas.94.22.11911.
↑ Pethica, R. B.. Evolutionarily consistent families in SCOP: Sequence, structure and function. BMC Structural Biology 12 (2012). p. 27. doi:10.1186/1472-6807-12-27.
↑ Xia, Y.. Ab initio construction of protein tertiary structures using a hierarchical approach. Journal of Molecular Biology 300 (1) (2000). p. 171–185. doi:10.1006/jmbi.2000.3835.
↑ Levitt Lab Server | Computational Structural Biology. Csb.stanford.edu. Retrieved 22 March 2017.
↑ Michael Levitt. Csb.stanford.edu\accessdate=2017-03-22.
↑ Van Noorden, Richard. Modellers react to chemistry award: Nobel Prize proves that theorists can measure up to experimenters. Nature 502 (7471) (2013). p. 280. doi:10.1038/502280a.

[whoswho-1] LEVITT, Prof. Michael. Who's Who. ukwhoswho.com 2003A & C Black, an imprint of Bloomsbury Publishing plc. (subscription needed)

[nobel_prize_chemistry-2] 2.0 ^2.1 ^2.2 ^2.3 Siegel-Itzkovich, Judy (9 October 2013). "Two American Israelis and US jew share Nobel Prize in Chemistry". The Jerusalem Post. http://www.jpost.com/Jewish-World/Jewish-Features/Israeli-scientists-awarded-Nobel-Prize-in-Chemistry-328246. Retrieved 12 November 2017.

[membo-3] Anon. Michael Levitt EMBO profile. people.embo.org (1983). Heidelberg: European Molecular Biology Organization.

[fellows-4] Anon. ISCB Fellows. iscb.org (2017)International Society for Computational Biology.

[5] Levitt, M.. The birth of computational structural biology. Nature Structural Biology 8 (5) (2001). p. 392–393. doi:10.1038/87545.

[6] Diamond, R.. A refinement of the structure of lysozyme. Biochemical Journal 125 (4) (1971). p. 92P. doi:10.1042/bj1250092Pa.

[7] Daggett, V.. Protein Unfolding Pathways Explored Through Molecular Dynamics Simulations. Journal of Molecular Biology 232 (2) (1993). p. 600–619. doi:10.1006/jmbi.1993.1414.

[8] Gerstein, M.. A structural census of the current population of protein sequences. PNAS 94 (22) (1997). p. 11911–11916. doi:10.1073/pnas.94.22.11911.

[9] Pethica, R. B.. Evolutionarily consistent families in SCOP: Sequence, structure and function. BMC Structural Biology 12 (2012). p. 27. doi:10.1186/1472-6807-12-27.

[10] Xia, Y.. Ab initio construction of protein tertiary structures using a hierarchical approach. Journal of Molecular Biology 300 (1) (2000). p. 171–185. doi:10.1006/jmbi.2000.3835.

[11] Levitt Lab Server | Computational Structural Biology. Csb.stanford.edu. Retrieved 22 March 2017.

[12] Michael Levitt. Csb.stanford.edu\accessdate=2017-03-22.

[13] Van Noorden, Richard. Modellers react to chemistry award: Nobel Prize proves that theorists can measure up to experimenters. Nature 502 (7471) (2013). p. 280. doi:10.1038/502280a.

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