Physics Today: The Royal Swedish Academy of Sciences has decided to award the Nobel Prize in Chemistry for 2009 jointly to
Venkatraman Ramakrishnan, MRC Laboratory of Molecular Biology, Cambridge,United Kingdom
Thomas A. Steitz, Yale University, New Haven, CT, USA
Ada E. Yonath, Weizmann Institute of Science, Rehovot, Israel
"for studies of the structure and function of the ribosome."
Inside every cell in all organisms, there are DNA molecules. They contain the blueprints for how a human being, a plant, or a bacterium looks and functions.
The DNA is transformed into living matter through the work of ribosomes. Based upon the information in DNA, ribosomes make the chemistry of life: proteins, such as oxygen-transporting hemoglobin, antibodies of the immune system, hormones such as insulin, the collagen of the skin, or enzymes that break down sugar.
There are tens of thousands of proteins in the body and they all have different forms and functions.
Ramakrishnan, Steitz, and Yonath discovered what the ribosome looks like and how it functions at the atomic level.
All three used X-ray crystallography to map the position for each and every one of the hundreds of thousands of atoms that make up the ribosome and created 3D models that show how different antibiotics bind to the ribosome. X-ray crystallography is a fundamental research tool in biophysics and chemistry, and has resulted in a number of Nobel Prizes.
"Today's award is one of the great stories in biophysics," says Jason Bardi, a spokesperson for the American Institute of Physics (which publishes Physics Today). "People worked for years to get these structures, and for a long time, many in the field doubted whether it could even be done."
The ribosome is a massive protein, weighing in at 2.5 million atomic mass units (amu) and has a complicated structure.
Ribosomes are so big that they can often be spotted under electron microscopes but attempts to look at their structures using diffracted light of much shorter X-wavelengths proved to be challenging.
When the hi-resolution images of ribosomes came out a decade ago by the three laureates, it was held as a significant breakthrough. "Frankly I was stunned," says Bardi. "The ribosomal structure most familiar to me previous to that was the one that adorned my "GENES IV" textbook in graduate school. It was a big purple blob—a molecular Barney. Now suddenly, I could see a thousand interwoven protein helices and finger-like sheets and an impossibly complicated tangle of RNA. It was a truly stunning image."
Paul Guinnessy
Related Physics Today Resources
A three-dimensional x-ray image of a single pair of human chromosomes, Charles Day, February 2009
Time-resolved macromolecular crystallography, Eric A. Galburt and Barry L. Stoddard, July 2001
Nobel Prize in Chemistry to Hauptman and Karle, Bruce Schechter, December 1985
Aaron Klug wins Nobel Prize in Chemistry, Bertram M. Schwarzschild, January 1983
Related Resources
Protein factory reveals Its secrets Chemical & Engineering News, February 2007
Venkatraman Ramakrishnan
Thomas A. Steitz
Ada E. Yonath
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Jason Bardi is right on with his comment that
"Today's award is one of the great stories in biophysics," says Jason Bardi, a spokesperson for the American Institute of Physics (which publishes Physics Today). "People worked for years to get these structures, and for a long time, many in the field doubted whether it could even be done."
One of this years prize winners, Ada Yonath, was a lone pioneer for many years developing the biochemical recipes for producing ribosome crystals capable of diffracting x-rays well enough to determine the structure, and for developing improved ways of acquiring the data with intense synchrotron sources before the x-rays changed the crystal. Others entered the field only after she showed promising results. It is a tribute to the Nobel committee that they have recognized the pioneer, although others eventually produced higher resolution results.