Each year the Nobel Foundation gives awards for accomplishments that benefit humanity. The 2004 Nobel Prize in Chemistry was awarded to biochemists Aaron Ciechanover and Avram Hershko (from Israel) and Irwin Rose (America) for ground-breaking work in understanding the molecular basis of diseases like cancer and Alzheimer's.1
The Nobel Laureates' award-winning research also benefits humanity in another way - one that extends beyond biochemistry and biomedicine. Their work provides powerful evidence that the cell's biochemical systems are the handiwork of a Creator.
During the early 1980s, the team identified one of the most important pathways used by the cell to break down vital molecular components, namely proteins. This destruction takes place when proteins are improperly made by the cell's machinery (which happens from time to time), when they become damaged as a result of normal wear and tear, or when they have outlived their usefulness.
Proteins, the workhorse molecules of life, take part in virtually every cellular structure and activity. Proteins catalyze (assist) chemical reactions, store and transport molecules, harvest chemical energy, and assemble and become part of the cell's structures.2 Simply put, every structure and activity inside the cell involves multiple proteins.
Proteins are chain-like molecules that fold into precise three-dimensional structures. The protein's three-dimensional shape uniquely determines its functional and/or structural role.3 If a protein's three-dimensional structure is compromised, the protein does not function properly and becomes a detriment to the cell.
Ciechanover, Hershko, and Rose discovered a biochemical system inside the cell that recognizes, and then "labels" structurally distorted proteins with a small protein called ubiquitin. This ubiquitin "tag" earmarks the nonfunctional protein for destruction and removal.4 This critical process keeps the cell's biochemical systems functioning efficiently, preventing the cell's interior from becoming cluttered with damaged, defective, and useless debris. Such removal also keeps harmful protein aggregates from forming inside the cell. Damaged proteins with distorted structures frequently combine with one another to form massive aggregates. As an example, protein aggregates are part of the etiology (cause) of Huntington's and Alzheimer's diseases.5
The "ubiquitination" of defective proteins functions as an elegant quality control and waste management system. Ubiquitin labels provide the cell's machinery with a way to distinguish properly functioning proteins from defective ones and to eliminate them from the cell. (The ubiquination pathway is just one of many quality control operations inside the cell.) Quality control procedures are hallmark characteristics of well-designed systems. By analogy, it is reasonable to conclude that the cell's quality control pathways, as well as the rest of the cell's biochemical systems, are designed as well. Perhaps the greater benefit for humanity in the team's laudable work is to highlight this truth.
- Jim Giles, "Molecular Kiss of Death," News@Nature.com, http://www.nature.com/news/2004/04/004/full/041004-9.html, accessed October 6, 2004; "Nobel Prize in Chemistry: Proteins Labeled for Destruction," Sciencedaily.com, http://www.sciencedaily.com/releases/2004/10/04/006084215.htm, accessed October 7, 2004.
- Robert C. Bohinksi, Modern Concepts in Biochemistry, 4th ed. (Boston: Allyn and Bacon, 1983), 86-87.
- Harvey Lodish et al., Molecular Cell Biology, 4th ed. (New York: W. H. Freeman, 2000), 54-60.
- Lodish et al., 66-67.
- Lodish et al., 67.