The 2002 Nobel Prize for Chemistry

Krishna Jani, Tanya Jayaram, Jordyn Kerner

What is the Nobel Prize, actually?

The Nobel Prize was founded by Alfred Nobel, a famous scientist, inventor, and businessman. In his last will and testament, he wished to have his fortune to be awarded to people who had brought greatness to humanity, in the fields of physics, chemistry, peace, literature, physiology, and medicine. Since 1901 the Nobel Prize has been awarded to thousands of accomplished people, and their discoveries and/or inventions have changed the way that humanity works.

Nobel Prize for Chemistry in 2002

As described in Alfred Nobel's will, the Nobel Prize in Chemistry was to be awarded to "the person who shall have made the most important chemical discovery or improvement." John B. Fenn, Koichi Tanaka, and Kurt Wüthrich received the Nobel Prize in Chemistry in 2002 for developing ways to correctly identify structures of macromolecules (molecules that are larger than average, such as proteins).

Who Won?

All three recipients researched physical chemical methodology -- the study of developing methods to further understand physical aspects of chemistry.

What Did They Do?

They created ways to correctly identify structures of macromolecules (molecules that are larger than average, such as proteins).

Using Mass Spectrometry

The only way to identify a substance was to use mass spectrometry -- a way of identifying a substance by using its mass. However, this method could only be used for small or medium sized molecules. John B. Fenn then introduced the electrospray ionization (ESI) method (shown below), where the sample of substance is sprayed using a strong electrical field. This breaks the substance down into a cloud of hovering ions which makes it easier to calculate the mass of the macromolecule.

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Mass spectrometry Animation

Koichi Tanaka also introduced the soft laser desorption (SLD) method (shown below), where an intense laser beam is transmitted to the substance, which forces the ions to separate. Similarly, this method makes it easier to calculate the mass of the macromolecule.

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Using Nuclear Magnetic Resonance

Nuclear magnetic resonance (NMR) is an occurrence where a nucleus of a cell can absorb and emit electromagnetic radiation. Kurt Wüthrich introduced the idea to use NMR to identify structures of macromolecules. This was done by pairing each individual NMR signal emitted from a substance with the right proton in the substance. One can compare this to knowing all the measurements of a house and being able to build the house. Similarly, if one knows all of the distances between molecules in a protein, they would be able to determine its structure (shown below).

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Why Did They Win?

The joint works of John B. Fenn and Koichi Tanaka in the field of improving mass spectrometry opened new doors for chemists. Previously, chemists could only use the mass spectrometer on small and medium sized molecules, but Fenn's idea of electrospray ionization allowed the mass and charge ratio to become small enough to be analyzed in a regular mass spectrometer. Tanaka created a similar result but by a different method by using the soft laser desorption method in order to break apart the connections between the molecules. The work of Tanaka and Fenn improved the work of biochemistry in the present, allowing for them to analyze macromolecules in greater detail. Their research helped identify diseases such as malaria and certain cancers.

Kurt Wüthrich’s idea to use the nuclear magnetic resonance spectroscopy to extend to even analyze proteins of macromolecules won him the second part of the 2002 Nobel Prize in Chemistry. His research allowed for macromolecule structures to be identified more accurately. The resulting protein image could then be used in studies of its structure and specifics such as in DNA.

Today chemists are using this research to identify the properties of unknown or questionable macromolecules. The sum of all of their works allowed for chemists to now be able to accurately identify what protein a sample contains and even produce a 3D image of the proteins used and identify their functions.