doi.bio/m_levitt


Michael Levitt

Michael Levitt (born 9 May 1947), FRS, is a South African-born biophysicist and structural biologist known for his work in molecular dynamics simulations and computational biology. He is currently a professor at Stanford University in California, a position he has held since 1987.

Early Life and Education

Levitt was born in Pretoria, South Africa, to a Jewish family from Lithuania. He attended Sunnyside Primary School and then Pretoria Boys High School between England when he was 15. He studied applied mathematics at the University of Pretoria and later received a Bachelor's degree in physics from King's College London in 1967. He went on to obtain a [[Doctor of Philosophy">PhD in computational biology from Peterhouse, Cambridge in 1971.

Career

Michael Levitt's career began at the Weizmann Institute of Science in Rehovot, Israel, where he was a visiting fellow from postdoctoral fellow at the MRC Laboratory of Molecular Biology from [[1972] to [1974]. During this time, he also held a position as a staff scientist at the laboratory from [[1974] to [1979].

In 1979, Levitt became an associate professor in chemical physics at the Weizmann Institute, and he left as a full professor in 1987. He then joined Stanford University as a professor of structural biology, where he has remained ever since.

Levitt is known for being one of the first researchers to conduct [[molecular dynamics">molecular dynamics simulations of [[DNA] and proteins. He developed the first software for this purpose and has made significant contributions to the field of computational biology. He has also worked on simplified representations of protein structure and the development of scoring systems for large-scale sequence-structure comparisons.

Awards and Honours

Michael Levitt received the 2013 Nobel Prize in Chemistry for "the development of multiscale models for complex chemical systems", which he shared with Martin Karplus and Arieh Warshel. He has also been recognised with numerous other awards, including:

COVID-19 Pandemic

During the COVID-19 pandemic, Levitt gained attention for his predictions and comments about the spread of the disease. While some of his early predictions were accurate, such as the decline of cases in China, he also made incorrect predictions, including the outbreak duration in the United States. He has also raised concerns about the potential negative impacts of lockdown measures on economic activity, suicide rates, and abuse rates.

Google Scholar Profile

M Levitt)

Google Scholar

Michael Levitt Structural Biology, Stanford University http://csb.stanford.edu/levitt/ Theoretical studies of enzymic reactions: dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme A Warshel, M Levitt Journal of molecular biology 103 (2), 227-249, 1976 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:u5HHmVD_uO8C Cited by: 5353

Conformations of immunoglobulin hypervariable regions C Chothia, AM Lesk, A Tramontano, M Levitt, SJ Smith-Gill, G Air, S Sheriff, … Nature 342 (6252), 877-883, 1989 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:d1gkVwhDpl0C Cited by: 1985

Structural patterns in globular proteins M Levitt, C Chothia Nature 261 (5561), 552-558, 1976 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:u-x6o8ySG0sC Cited by: 1645

A simplified representation of protein conformations for rapid simulation of protein folding M Levitt Journal of molecular biology 104 (1), 59-107, 1976 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:9yKSN-GCB0IC Cited by: 1455

A humanized antibody that binds to the interleukin 2 receptor. C Queen, WP Schneider, HE Selick, PW Payne, NF Landolfi, JF Duncan, … Proceedings of the National Academy of Sciences 86 (24), 10029-10033, 1989 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:2osOgNQ5qMEC Cited by: 1447

Computer simulation of protein folding M Levitt, A Warshel Nature 253 (5494), 694-698, 1975 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:IjCSPb-OGe4C Cited by: 1408

Conformation of amino acid side-chains in proteins J Janin, S Wodak, M Levitt, B Maigret Journal of molecular biology 125 (3), 357-386, 1978 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:qjMakFHDy7sC Cited by: 1006

Structure of nucleosome core particles of chromatin JT Finch, LC Lutter, D Rhodes, RS Brown, B Rushton, M Levitt, A Klug Nature 269 (5623), 29-36, 1977 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:UeHWp8X0CEIC Cited by: 981

Protein normal-mode dynamics: trypsin inhibitor, crambin, ribonuclease and lysozyme M Levitt, C Sander, PS Stern Journal of molecular biology 181 (3), 423-447, 1985 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:Tyk-4Ss8FVUC Cited by: 878

Aromatic rings act as hydrogen bond acceptors M Levitt, MF Perutz Journal of molecular biology 201 (4), 751-754, 1988 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:Y0pCki6q_DkC Cited by: 862

Conformational preferences of amino acids in globular proteins M Levitt Biochemistry 17 (20), 4277-4285, 1978 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:W7OEmFMy1HYC Cited by: 856

Accurate modeling of protein conformation by automatic segment matching M Levitt Journal of molecular biology 226 (2), 507-533, 1992 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:zYLM7Y9cAGgC Cited by: 755

The ASTRAL compendium in 2004 JM Chandonia, G Hon, NS Walker, L Lo Conte, P Koehl, M Levitt, … Nucleic acids research 32 (suppl1), D189-D192, 2004 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxz_OGgAAAAJ:eQOLeE2rZwMC Cited by: 724

Helix to helix packing in proteins C Chothia, M Levitt, D Richardson Journal of molecular biology 145 (1), 215-250, 1981 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:WF5omc3nYNoC Cited by: 699

Calibration and testing of a water model for simulation of the molecular dynamics of proteins and nucleic acids in solution M Levitt, M Hirshberg, R Sharon, KE Laidig, V Daggett The Journal of Physical Chemistry B 101 (25), 5051-5061, 1997 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:roLk4NBRz8UC Cited by: 664

Refinement of protein conformations using a macromolecular energy minimization procedure M Levitt, S Lifson Journal of molecular biology 46 (2), 269-279, 1969 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:MXK_kJrjxJIC Cited by: 636

Automatic identification of secondary structure in globular proteins M Levitt, J Greer Journal of molecular biology 114 (2), 181-239, 1977 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:ufrVoPGSRksC Cited by: 628

Accurate simulation of protein dynamics in solution. M Levitt, R Sharon Proceedings of the National Academy of Sciences 85 (20), 7557-7561, 1988 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:LkGwnXOMwfcC Cited by: 615

Potential energy function and parameters for simulations of the molecular dynamics of proteins and nucleic acids in solution M Levitt, M Hirshberg, R Sharon, V Daggett Computer physics communications 91 (1-3), 215-231, 1995 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:UebtZRa9Y70C Cited by: 596

Energy functions that discriminate X-ray and near-native folds from well-constructed decoys B Park, M Levitt Journal of molecular biology 258 (2), 367-392, 1996 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:_FxGoFyzp5QC Cited by: 516

Co-authors

Patrice Koehl NRAo--UAAAAJ

Mark Gerstein YvjuUugAAAAJ

Gunnar F. Schröder SdqGIOYAAAAJ

Enoch S. Huang DUGvmakAAAAJ

Yu (Brandon) Xia McgMhW0AAAAJ

Ram Samudrala a45-Ka8AAAAJ

Boris Fain elVfY5wAAAAJ

Rachel Kolodny WTihfsYAAAAJ

Chris Sander 4R7_wW8AAAAJ

Peter Minary ruz8HrEAAAAJ

David Hinds epTHxM0AAAAJ

Dahlia R Weiss OiXkFpIAAAAJ

Junjie Zhang xLuMADUAAAAJ

David A. Bushnell 2yVAzfgAAAAJ

Steven J Ludtke iJQcLr0AAAAJ

Xuhui Huang cDpFo0oAAAAJ

Adelene Sim 4RDPMzgAAAAJ

João PGLM Rodrigues UeXRdzQAAAAJ

Gaurav Chopra wEo9gf4AAAAJ

Dong Wang 7vkluXEAAAAJ

Google Scholar

Michael Levitt Structural Biology, Stanford University http://csb.stanford.edu/levitt/ Theoretical studies of enzymic reactions: dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme A Warshel, M Levitt Journal of molecular biology 103 (2), 227-249, 1976 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:u5HHmVD_uO8C Cited by: 5353

Conformations of immunoglobulin hypervariable regions C Chothia, AM Lesk, A Tramontano, M Levitt, SJ Smith-Gill, G Air, S Sheriff, … Nature 342 (6252), 877-883, 1989 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:d1gkVwhDpl0C Cited by: 1985

Structural patterns in globular proteins M Levitt, C Chothia Nature 261 (5561), 552-558, 1976 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:u-x6o8ySG0sC Cited by: 1645

A simplified representation of protein conformations for rapid simulation of protein folding M Levitt Journal of molecular biology 104 (1), 59-107, 1976 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:9yKSN-GCB0IC Cited by: 1455

A humanized antibody that binds to the interleukin 2 receptor. C Queen, WP Schneider, HE Selick, PW Payne, NF Landolfi, JF Duncan, … Proceedings of the National Academy of Sciences 86 (24), 10029-10033, 1989 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:2osOgNQ5qMEC Cited by: 1447

Computer simulation of protein folding M Levitt, A Warshel Nature 253 (5494), 694-698, 1975 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:IjCSPb-OGe4C Cited by: 1408

Conformation of amino acid side-chains in proteins J Janin, S Wodak, M Levitt, B Maigret Journal of molecular biology 125 (3), 357-386, 1978 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:qjMakFHDy7sC Cited by: 1006

Structure of nucleosome core particles of chromatin JT Finch, LC Lutter, D Rhodes, RS Brown, B Rushton, M Levitt, A Klug Nature 269 (5623), 29-36, 1977 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:UeHWp8X0CEIC Cited by: 981

Protein normal-mode dynamics: trypsin inhibitor, crambin, ribonuclease and lysozyme M Levitt, C Sander, PS Stern Journal of molecular biology 181 (3), 423-447, 1985 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:Tyk-4Ss8FVUC Cited by: 878

Aromatic rings act as hydrogen bond acceptors M Levitt, MF Perutz Journal of molecular biology 201 (4), 751-754, 1988 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:Y0pCki6q_DkC Cited by: 862

Conformational preferences of amino acids in globular proteins M Levitt Biochemistry 17 (20), 4277-4285, 1978 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:W7OEmFMy1HYC Cited by: 856

Accurate modeling of protein conformation by automatic segment matching M Levitt Journal of molecular biology 226 (2), 507-533, 1992 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:zYLM7Y9cAGgC Cited by: 755

The ASTRAL compendium in 2004 JM Chandonia, G Hon, NS Walker, L Lo Conte, P Koehl, M Levitt, … Nucleic acids research 32 (suppl1), D189-D192, 2004 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxz_OGgAAAAJ:eQOLeE2rZwMC Cited by: 724

Helix to helix packing in proteins C Chothia, M Levitt, D Richardson Journal of molecular biology 145 (1), 215-250, 1981 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:WF5omc3nYNoC Cited by: 699

Calibration and testing of a water model for simulation of the molecular dynamics of proteins and nucleic acids in solution M Levitt, M Hirshberg, R Sharon, KE Laidig, V Daggett The Journal of Physical Chemistry B 101 (25), 5051-5061, 1997 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:roLk4NBRz8UC Cited by: 664

Refinement of protein conformations using a macromolecular energy minimization procedure M Levitt, S Lifson Journal of molecular biology 46 (2), 269-279, 1969 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:MXK_kJrjxJIC Cited by: 636

Automatic identification of secondary structure in globular proteins M Levitt, J Greer Journal of molecular biology 114 (2), 181-239, 1977 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:ufrVoPGSRksC Cited by: 628

Accurate simulation of protein dynamics in solution. M Levitt, R Sharon Proceedings of the National Academy of Sciences 85 (20), 7557-7561, 1988 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:LkGwnXOMwfcC Cited by: 615

Potential energy function and parameters for simulations of the molecular dynamics of proteins and nucleic acids in solution M Levitt, M Hirshberg, R Sharon, V Daggett Computer physics communications 91 (1-3), 215-231, 1995 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:UebtZRa9Y70C Cited by: 596

Energy functions that discriminate X-ray and near-native folds from well-constructed decoys B Park, M Levitt Journal of molecular biology 258 (2), 367-392, 1996 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:_FxGoFyzp5QC Cited by: 516

Co-authors

Patrice Koehl googlescholarauthor_id:NRAo--UAAAAJ

Mark Gerstein googlescholarauthor_id:YvjuUugAAAAJ

Gunnar F. Schröder googlescholarauthor_id:SdqGIOYAAAAJ

Enoch S. Huang googlescholarauthor_id:DUGvmakAAAAJ

Yu (Brandon) Xia googlescholarauthor_id:McgMhW0AAAAJ

Ram Samudrala googlescholarauthor_id:a45-Ka8AAAAJ

Boris Fain googlescholarauthor_id:elVfY5wAAAAJ

Rachel Kolodny googlescholarauthor_id:WTihfsYAAAAJ

Chris Sander googlescholarauthorid:4R7wW8AAAAJ

Peter Minary googlescholarauthor_id:ruz8HrEAAAAJ

David Hinds googlescholarauthor_id:epTHxM0AAAAJ

Dahlia R Weiss googlescholarauthor_id:OiXkFpIAAAAJ

Junjie Zhang googlescholarauthor_id:xLuMADUAAAAJ

David A. Bushnell googlescholarauthor_id:2yVAzfgAAAAJ

Steven J Ludtke googlescholarauthor_id:iJQcLr0AAAAJ

Xuhui Huang googlescholarauthor_id:cDpFo0oAAAAJ

Adelene Sim googlescholarauthor_id:4RDPMzgAAAAJ

João PGLM Rodrigues googlescholarauthor_id:UeXRdzQAAAAJ

Gaurav Chopra googlescholarauthor_id:wEo9gf4AAAAJ

Dong Wang googlescholarauthor_id:7vkluXEAAAAJ

Google Scholar

Michael Levitt Structural Biology, Stanford University http://csb.stanford.edu/levitt/ Theoretical studies of enzymic reactions: dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme A Warshel, M Levitt Journal of molecular biology 103 (2), 227-249, 1976 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:u5HHmVD_uO8C Cited by: 5353

Conformations of immunoglobulin hypervariable regions C Chothia, AM Lesk, A Tramontano, M Levitt, SJ Smith-Gill, G Air, S Sheriff, … Nature 342 (6252), 877-883, 1989 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:d1gkVwhDpl0C Cited by: 1985

Structural patterns in globular proteins M Levitt, C Chothia Nature 261 (5561), 552-558, 1976 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:u-x6o8ySG0sC Cited by: 1645

A simplified representation of protein conformations for rapid simulation of protein folding M Levitt Journal of molecular biology 104 (1), 59-107, 1976 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:9yKSN-GCB0IC Cited by: 1455

A humanized antibody that binds to the interleukin 2 receptor. C Queen, WP Schneider, HE Selick, PW Payne, NF Landolfi, JF Duncan, … Proceedings of the National Academy of Sciences 86 (24), 10029-10033, 1989 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:2osOgNQ5qMEC Cited by: 1447

Computer simulation of protein folding M Levitt, A Warshel Nature 253 (5494), 694-698, 1975 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:IjCSPb-OGe4C Cited by: 1408

Conformation of amino acid side-chains in proteins J Janin, S Wodak, M Levitt, B Maigret Journal of molecular biology 125 (3), 357-386, 1978 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:qjMakFHDy7sC Cited by: 1006

Structure of nucleosome core particles of chromatin JT Finch, LC Lutter, D Rhodes, RS Brown, B Rushton, M Levitt, A Klug Nature 269 (5623), 29-36, 1977 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:UeHWp8X0CEIC Cited by: 981

Protein normal-mode dynamics: trypsin inhibitor, crambin, ribonuclease and lysozyme M Levitt, C Sander, PS Stern Journal of molecular biology 181 (3), 423-447, 1985 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:Tyk-4Ss8FVUC Cited by: 878

Aromatic rings act as hydrogen bond acceptors M Levitt, MF Perutz Journal of molecular biology 201 (4), 751-754, 1988 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:Y0pCki6q_DkC Cited by: 862

Conformational preferences of amino acids in globular proteins M Levitt Biochemistry 17 (20), 4277-4285, 1978 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:W7OEmFMy1HYC Cited by: 856

Accurate modeling of protein conformation by automatic segment matching M Levitt Journal of molecular biology 226 (2), 507-533, 1992 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:zYLM7Y9cAGgC Cited by: 755

The ASTRAL compendium in 2004 JM Chandonia, G Hon, NS Walker, L Lo Conte, P Koehl, M Levitt, … Nucleic acids research 32 (suppl1), D189-D192, 2004 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxz_OGgAAAAJ:eQOLeE2rZwMC Cited by: 724

Helix to helix packing in proteins C Chothia, M Levitt, D Richardson Journal of molecular biology 145 (1), 215-250, 1981 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:WF5omc3nYNoC Cited by: 699

Calibration and testing of a water model for simulation of the molecular dynamics of proteins and nucleic acids in solution M Levitt, M Hirshberg, R Sharon, KE Laidig, V Daggett The Journal of Physical Chemistry B 101 (25), 5051-5061, 1997 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:roLk4NBRz8UC Cited by: 664

Refinement of protein conformations using a macromolecular energy minimization procedure M Levitt, S Lifson Journal of molecular biology 46 (2), 269-279, 1969 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:MXK_kJrjxJIC Cited by: 636

Automatic identification of secondary structure in globular proteins M Levitt, J Greer Journal of molecular biology 114 (2), 181-239, 1977 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:ufrVoPGSRksC Cited by: 628

Accurate simulation of protein dynamics in solution. M Levitt, R Sharon Proceedings of the National Academy of Sciences 85 (20), 7557-7561, 1988 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:LkGwnXOMwfcC Cited by: 615

Potential energy function and parameters for simulations of the molecular dynamics of proteins and nucleic acids in solution M Levitt, M Hirshberg, R Sharon, V Daggett Computer physics communications 91 (1-3), 215-231, 1995 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:UebtZRa9Y70C Cited by: 596

Energy functions that discriminate X-ray and near-native folds from well-constructed decoys B Park, M Levitt Journal of molecular biology 258 (2), 367-392, 1996 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:_FxGoFyzp5QC Cited by: 516

Co-authors

Patrice Koehl googlescholarauthorid patricekoehl.md:NRAo--UAAAAJ

Mark Gerstein googlescholarauthorid markgerstein.md:YvjuUugAAAAJ

Gunnar F. Schröder googlescholarauthorid gunnarf._schröder.md:SdqGIOYAAAAJ

Enoch S. Huang googlescholarauthorid enochs._huang.md:DUGvmakAAAAJ

Yu (Brandon) Xia googlescholarauthorid yu(brandon)_xia.md:McgMhW0AAAAJ

Ram Samudrala googlescholarauthorid ramsamudrala.md:a45-Ka8AAAAJ

Boris Fain googlescholarauthorid borisfain.md:elVfY5wAAAAJ

Rachel Kolodny googlescholarauthorid rachelkolodny.md:WTihfsYAAAAJ

Chris Sander googlescholarauthorid chrissander.md:4R7_wW8AAAAJ

Peter Minary googlescholarauthorid peterminary.md:ruz8HrEAAAAJ

David Hinds googlescholarauthorid davidhinds.md:epTHxM0AAAAJ

Dahlia R Weiss googlescholarauthorid dahliar_weiss.md:OiXkFpIAAAAJ

Junjie Zhang googlescholarauthorid junjiezhang.md:xLuMADUAAAAJ

David A. Bushnell googlescholarauthorid davida._bushnell.md:2yVAzfgAAAAJ

Steven J Ludtke googlescholarauthorid stevenj_ludtke.md:iJQcLr0AAAAJ

Xuhui Huang googlescholarauthorid xuhuihuang.md:cDpFo0oAAAAJ

Adelene Sim googlescholarauthorid adelenesim.md:4RDPMzgAAAAJ

João PGLM Rodrigues googlescholarauthorid joãopglm_rodrigues.md:UeXRdzQAAAAJ

Gaurav Chopra googlescholarauthorid gauravchopra.md:wEo9gf4AAAAJ

Dong Wang googlescholarauthorid dongwang.md:7vkluXEAAAAJ

Google Scholar

Michael Levitt

Structural Biology, Stanford University

http://csb.stanford.edu/levitt/

Theoretical studies of enzymic reactions: dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme A Warshel, M Levitt Journal of molecular biology 103 (2), 227-249, 1976 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:u5HHmVD_uO8C

Conformations of immunoglobulin hypervariable regions C Chothia, AM Lesk, A Tramontano, M Levitt, SJ Smith-Gill, G Air, S Sheriff, … Nature 342 (6252), 877-883, 1989 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:d1gkVwhDpl0C

Structural patterns in globular proteins M Levitt, C Chothia Nature 261 (5561), 552-558, 1976 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:u-x6o8ySG0sC

A simplified representation of protein conformations for rapid simulation of protein folding M Levitt Journal of molecular biology 104 (1), 59-107, 1976 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:9yKSN-GCB0IC

A humanized antibody that binds to the interleukin 2 receptor. C Queen, WP Schneider, HE Selick, PW Payne, NF Landolfi, JF Duncan, … Proceedings of the National Academy of Sciences 86 (24), 10029-10033, 1989 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:2osOgNQ5qMEC

Computer simulation of protein folding M Levitt, A Warshel Nature 253 (5494), 694-698, 1975 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:IjCSPb-OGe4C

Conformation of amino acid side-chains in proteins J Janin, S Wodak, M Levitt, B Maigret Journal of molecular biology 125 (3), 357-386, 1978 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:qjMakFHDy7sC

Structure of nucleosome core particles of chromatin JT Finch, LC Lutter, D Rhodes, RS Brown, B Rushton, M Levitt, A Klug Nature 269 (5623), 29-36, 1977 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:UeHWp8X0CEIC

Protein normal-mode dynamics: trypsin inhibitor, crambin, ribonuclease and lysozyme M Levitt, C Sander, PS Stern Journal of molecular biology 181 (3), 423-447, 1985 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:Tyk-4Ss8FVUC

Aromatic rings act as hydrogen bond acceptors M Levitt, MF Perutz Journal of molecular biology 201 (4), 751-754, 1988 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:Y0pCki6q_DkC

Conformational preferences of amino acids in globular proteins M Levitt Biochemistry 17 (20), 4277-4285, 1978 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:W7OEmFMy1HYC

Accurate modeling of protein conformation by automatic segment matching M Levitt Journal of molecular biology 226 (2), 507-533, 1992 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:zYLM7Y9cAGgC

The ASTRAL compendium in 2004 JM Chandonia, G Hon, NS Walker, L Lo Conte, P Koehl, M Levitt, … Nucleic acids research 32 (suppl1), D189-D192, 2004 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxz_OGgAAAAJ:eQOLeE2rZwMC

Helix to helix packing in proteins C Chothia, M Levitt, D Richardson Journal of molecular biology 145 (1), 215-250, 1981 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:WF5omc3nYNoC

Calibration and testing of a water model for simulation of the molecular dynamics of proteins and nucleic acids in solution M Levitt, M Hirshberg, R Sharon, KE Laidig, V Daggett The Journal of Physical Chemistry B 101 (25), 5051-5061, 1997 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:roLk4NBRz8UC

Refinement of protein conformations using a macromolecular energy minimization procedure M Levitt, S Lifson Journal of molecular biology 46 (2), 269-279, 1969 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:MXK_kJrjxJIC

Automatic identification of secondary structure in globular proteins M Levitt, J Greer Journal of molecular biology 114 (2), 181-239, 1977 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:ufrVoPGSRksC

Accurate simulation of protein dynamics in solution. M Levitt, R Sharon Proceedings of the National Academy of Sciences 85 (20), 7557-7561, 1988 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:LkGwnXOMwfcC

Potential energy function and parameters for simulations of the molecular dynamics of proteins and nucleic acids in solution M Levitt, M Hirshberg, R Sharon, V Daggett Computer physics communications 91 (1-3), 215-231, 1995 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:UebtZRa9Y70C

Energy functions that discriminate X-ray and near-native folds from well-constructed decoys B Park, M Levitt Journal of molecular biology 258 (2), 367-392, 1996 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=zxzOGgAAAAJ&citationforview=zxzOGgAAAAJ:_FxGoFyzp5QC

Co-authors

Patrice Koehl googlescholarauthorid patricekoehl.md:NRAo--UAAAAJ

Mark Gerstein googlescholarauthorid markgerstein.md:YvjuUugAAAAJ

Gunnar F. Schröder googlescholarauthorid gunnarf._schröder.md:SdqGIOYAAAAJ

Enoch S. Huang googlescholarauthorid enochs._huang.md:DUGvmakAAAAJ

Yu (Brandon) Xia googlescholarauthorid yu(brandon)_xia.md:McgMhW0AAAAJ

Ram Samudrala googlescholarauthorid ramsamudrala.md:a45-Ka8AAAAJ

Boris Fain googlescholarauthorid borisfain.md:elVfY5wAAAAJ

Rachel Kolodny googlescholarauthorid rachelkolodny.md:WTihfsYAAAAJ

Chris Sander googlescholarauthorid chrissander.md:4R7_wW8AAAAJ

Peter Minary googlescholarauthorid peterminary.md:ruz8HrEAAAAJ

David Hinds googlescholarauthorid davidhinds.md:epTHxM0AAAAJ

Dahlia R Weiss googlescholarauthorid dahliar_weiss.md:OiXkFpIAAAAJ

Junjie Zhang googlescholarauthorid junjiezhang.md:xLuMADUAAAAJ

David A. Bushnell googlescholarauthorid davida._bushnell.md:2yVAzfgAAAAJ

Steven J Ludtke googlescholarauthorid stevenj_ludtke.md:iJQcLr0AAAAJ

Xuhui Huang googlescholarauthorid xuhuihuang.md:cDpFo0oAAAAJ

Adelene Sim googlescholarauthorid adelenesim.md:4RDPMzgAAAAJ

João PGLM Rodrigues googlescholarauthorid joãopglm_rodrigues.md:UeXRdzQAAAAJ

Gaurav Chopra googlescholarauthorid gauravchopra.md:wEo9gf4AAAAJ

Dong Wang googlescholarauthorid dongwang.md:7vkluXEAAAAJ

Youtube Videos

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AI-powered Drug Discovery lecture by Dr. Michael Levitt, 2013 Nobel Laureate in Chemistry

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M Levitt #2 Concepts of curve fitting

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Julie M. Levitt, MD

Youtube Title: M Levitt short videos #1 Exponential Growth

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M Levitt short videos #1 Exponential Growth

Youtube Title: Fireside chat with Michael Levitt: acceleration of AI-powered drug discovery

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Fireside chat with Michael Levitt: acceleration of AI-powered drug discovery

Youtube Title: Genes, environment and responsibility for behaviour - Dr Mairi Levitt

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Genes, environment and responsibility for behaviour - Dr Mairi Levitt

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Youtube Title: Joseph Gordon-Levitt's "Rhythm Nation" vs. Anthony Mackie's "2 Legit 2 Quit" | Lip Sync Battle

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Joseph Gordon-Levitt's "Rhythm Nation" vs. Anthony Mackie's "2 Legit 2 Quit" | Lip Sync Battle

Youtube Title: Dec 17 2020 Michael Levitt Editted V1

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Dec 17 2020 Michael Levitt Editted V1

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Levitt LA 2024 pres. Indie Soundscape

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A Magic Moment with Joseph Gordon-Levitt

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Tommy Shelby meets with Mr. Levitt from the London Times || S05E01 || PEAKY BLINDERS

Youtube Title: The Witch of Deacon Hill by Paul M. Levitt. BBC RADIO DRAMA

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The Witch of Deacon Hill by Paul M. Levitt. BBC RADIO DRAMA

Youtube Title: Prof. Michael Levitt | Direct | COVID-19: Choices and Consequences

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Chaim Malespin

Youtube Title: Levitt Workshop: Critical-Constructivist Grounded Theory Research: The Study of Meaning in Context

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Youtube Channel Name: SQIP Annual Conference 2022

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Levitt Workshop: Critical-Constructivist Grounded Theory Research: The Study of Meaning in Context

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What's up cats up i'm levitt