Michael Levitt

Michael Levitt ( born May 9, 1947 in Pretoria) is a native of South Africa chemist with American, British and Israeli citizenship. On October 9, 2013, the program was awarded jointly with Martin Karplus and Arieh Warshel the Nobel Prize in Chemistry "for the development of multi-scale models of complex chemical systems."

Training and research topics

Levitt studied physics in 1964 at King's College London with a Bachelor 's degree in 1967 and in 1971 at the Laboratory of Molecular Biology in Cambridge PhD in Biophysics ( Conformal Analysis of protein). As a post - graduate student, he was from 1972 to 1974 EMBO Fellow at the Weizmann Institute of Science in Shneior Lifson. 1974 to 1979 he was a scientist at the Laboratory of Molecular Biology in Cambridge and from 1977 to 1979 visiting scientist with Francis Crick at the Salk Institute in La Jolla, California. From 1979 he was professor of physical chemistry at the Weizmann Institute and from 1987 professor of structural biology at Stanford University. 1993 to 2004 he stood in front of the Department of Structural Biology at Stanford.

He was a visiting professor at the Weizmann Institute, the University of Paris and at the Ecole Normale Superieure ( Blaise Pascal Chair ).

He made important contributions to computer simulation, for example, by movement of proteins in solutions and protein folding. He dealt in addition to proteins with computer simulations for structural biology of RNA and DNA, and advanced methods of genome sequence analysis using the computer to generate information about the encoded proteins in the genome. Mostly, he worked with Arieh Warshel.

In 2001 he became a Fellow of the Royal Society, in 2002 the National Academy of Sciences and in 2010 the American Academy of Arts and Sciences.

He has been married since 1968 and has three children.


  • With S. Lifson: Refinement of protein conformations Using a Macromolecular Energy Minimization Procedure. In: Journal of Molecular Biology. Volume 46, 1969, pp. 269-279.
  • Detailed Molecular Model for Transfer Ribonucleic Acid. in: Nature. Volume 224, 1969, pp. 759-763.
  • With A. Warshel: Computer simulation of protein folding. In: Nature. Volume 253, 1975, pp. 694-698.
  • With A. Warshel: Theoretical Studies of Enzymic Reactions: Dielectric, Electrostatic and Steric Stabilization of the Carbonium Ion in the Reaction of Lysozyme. In: Journal of Molecular Biology. Volume 103, 1976, pp. 227-249.
  • With C. Chothia: Structural Patterns in Globular protein. In: Nature. Volume 261, 1976, pp. 552-558.
  • Simplified representation of protein conformations for rapid simulation of protein folding. In: Journal of Molecular Biology. Volume 104, 1976, pp. 59-107.
  • With J. T. Finch, L. C. Lutter, D. Rhodes, R. S. Brown, B. Rushton, A. Klug: Structure of the Nucleosome Core Particles of chromatin. In: Nature. Volume 269, 1977, pp. 29-35.
  • With A. Jack: Refinement of Large Structures by Simultaneous Minimization of Energy and R Factor. In: Acta Crystallogr. Volume A34, 1978, pp. 931-935.
  • With J. Janin, S. Wodak, B. Maigret: The Conformation of Amino Acid Side Chains in protein. In: Journal of Molecular Biology. Volume 125, 1978, pp. 357-386.
  • Protein Conformation, Dynamics and Folding by computer simulation. In: Annual Review of Biophysics and Bioengineering. Volume 11, 1982, p 251-271.
  • Protein Folding by Restrained Energy Minimization and Molecular Dynamics. In: Journal of Molecular Biology. Volume 170, 1983, pp. 723-764.
  • With Sharon R.: Accurate Simulation of Protein Dynamics in Solution. In: Proceedings of the National Academy of Sciences. Volume 85, 1988, pp. 7557-7561.
  • With C. Chothia, AM Lesk, A. Tramontano, SJ Smith -Gill, G. Air, S. Sheriff, EA Padlan, D. Davies, WR Tulip, PM Colman: The conformations of immunoglobulin hypervariable regions. In: Nature. Volume 342, 1989, pp. 877-883.
  • With C. Queen, WP Schneider, HE Selick, PW Payne, NF Landolfi, JF Duncan, NM Avdalovic, RP Junghans, TA Waldmann: A Humanized Antibody did Binds to the IL- 2 Receptor. In: Proceedings of the National Academy of Sciences. Volume 86, 1989, p 10029-10033.
  • With V. Daggett: Realistic simulation of Native Protein Dynamics in Solution and Beyond. In: Annual Review of Biophysics and Biomolecular Structure. Volume 22, 1993, pp. 353-380.
  • With V. Daggett: Protein Unfolding Pathways Explored Through Molecular Dynamics Simulations. In: Journal of Molecular Biology. Band 232, 1993, pp. 600-618.
  • DA Hinds: From structure to sequence and back again. In: Journal of Molecular Biology. Volume 258, 1996, pp. 201-209.
  • With M. Gerstein, E.S. Huang, S. Subbiah, J. Tsai: Protein Folding: The End Game. In: Annual Review of Biochemistry. Volume 66, 1997, pp. 549-579.
  • With Patrice Koehl: Protein topology and stability define the space of allowed sequences. In: Proceedings of the National Academy of Sciences. Volume 99, 2002, pp. 1280-1285.
  • With Y. Xia: Simulating protein evolution in sequence and Structure Space. In: Current Opinion in Structural Biology. Volume 14, 2004, pp. 202-207.
  • Nature of the protein universe. In: Proceedings of the National Academy of Sciences. Volume 106, 2009, pp. 11079-11084.
  • With M. Gerstein: Simulating water and the proteins of life. In: Scientific American. November 1998