Nobel Prize for Chemistry 2013
3go8 Crystal structure of a base-excision DNA repair enzyme, MutM (Entry 3go8)
4aol Crystal structure of eukaryotic chaperonin CCT. (Entry 2aol)
2iso DNA Polymerase beta (Entry 2iso)

The 2013 Nobel Prize was awarded for the development of multiscale models.

This year's Nobel Prize for Chemistry has been awarded to Martin Karplus, Michael Levitt and Arieh Warshel for the development of multiscale models for complex chemical systems.

In the 1970’s Karplus, Levitt and Warshel laid the foundation for powerful computer programs that model chemical behaviour and are used to understand and predict large complex chemical systems and reactions. Today, computers and theoretical models are essential components of every chemist’s and biologist’s toolbox.

In addition to developing computational methods, all three Nobel Laureates have experimentally determined structures and deposited them in the PDB. Recent examples are show in the right-hand pane.

Computer models underpin methods used for structure determination.

This year’s Nobel laureates have developed hybrid approaches that combined classical and quantum physics and they have shown how these can be used to successfully model dynamical properties of real biological systems, ranging from protein-folding to electron transfer reactions. Among other developments, such hybrid approaches have led to more accurate atomic force fields, a crucial component of structure determination by structural biology techniques, such as X-ray crystallography and NMR.

A personal account of Michael Levitt's contributions to structure determination.

PDBe’s Miri Hirschberg was Michael Levitt's first PhD student at the Department of Chemical Physics at the Weizmann Institute of Science, Israel. In 1987 Miri moved with Michael to Stanford University where she completed her PhD on nucleic acid simulations in water.

“Michael’s work has contributed extensively to the field of macromolecule structure and dynamics, from theoretical simulations to experimental structure determination” says Miri “the Jack and Levitt Real space refinement method was used extensively in the early years of X-ray crystallography, and more recently he has developed new methods for molecular replacement by exploring and assessing all possible arrangements of a structure in the crystal unit cell”.

The first Movie of Protein Molecular Dynamics simulated by Michael Levitt in 1979 is available on YouTube.

Timeline of structural biology related Nobel Prizes (Drag or double-click timeline to navigate.)

More than 20 structural biology-related Nobel Prizes have been awarded in the past 50 years.

The Foundation has awarded more than 20 Nobel Prizes to structural biologists in the past 50 years. These include the Nobel Prize for Chemistry in 1962 (for studies of the structures of globular proteins) to John Kendrew and Max Perutz and the Nobel Prize in Physiology or Medicine in the same year to Francis Crick, James Watson and Maurice Wilkins (for their studies of "The helical structure of DNA"). More recently, Robert Lefkowitz and Brian Kobilka were awarded the 2012 Nobel Prize in Chemistry for their studies of G-protein–coupled receptors.

The combined wealth of information generated by the structural biology community is freely available in The Protein Data Bank.

Information generated by the structural biology community, be it the atomic details of ribosomes, haemoglobin or any other protein or nucleic-acid molecules or complexes, is archived in the Protein Data Bank (PDB). The accumulated data in the PDB archive provides a wealth of knowledge on protein structure and function. The PDB archive was established in 1972 and is now managed by the four Worldwide Protein Data Bank (wwPDB) partners - RCSB and BMRB in the USA, PDBj in Japan and the Protein Data Bank in Europe (PDBe) at the European Bioinformatics Institute (EBI) in Cambridge, UK. The four partners ensure that the data is available to the wider scientific community for research and development in the field of biology and medicine.