THE COLLEGE HILL INDEPENDENT


Nobel Selections

the noblest nerds of 2009

by by Nick Werle

Physics
Were it not for this year’s Nobel laureates in physics, it is safe to say that no college student would find himself exposed to professors, parents, and future employers as a degenerate drunk. But we also wouldn’t have Facebook pictures.

Willard S. Boyle and George E. Smith were both researchers at Bell Labs in 1969 when they theorized, designed, and built the first charge-coupled device (CCD), a solid state, light transduction unit that replaced color film as the dominant form of image capture technology. When a light photon strikes the silicon surface grid of a CCD, it ejects electrons from the surface of the device. 

Albert Einstein won the 1921 Nobel Prize in physics for his work on this phenomenon, called the photoelectric effect. These ejected electrons form “charge bubbles,” which accumulate in the CCD’s grid and compose an analog representation of light intensities forming the image. Today, CCDs are used to capture images of space in the Hubble Space Telescope and Mars rovers, images of the body in micro-surgical tools, and images of college students’ drunk bodies in digital cameras.

The other half of the physics prize went to Charles K. Kao, who, working in London in 1966, figured out how to make fiber optic cables a viable communications technology. Before Kao’s work, glass fibers were not thought to be an effective medium for transmitting information because light signals seemed to dissipate after only about 20 meters. Kao determined that impurities in the glass attenuated light but that a fiber of higher purity could carry light pulses without such losses. Modern fiber optic cables can carry light signals over a kilometer while retaining 95 percent of the original signal strength. Today, more than a billion kilometers worth of Kao’s glass fibers carry data for communications, research, and Facebook photos around the world at the speed of light.

Physiology or medicine
The Swedish Academy of Sciences awarded this year’s Nobel Prize in Physiology or Medicine to a trio of biologists who unraveled the genetic mystery of telomeres, which are sections of repeating DNA patterns located at the end of each chromosome. Each time a cell’s DNA is copied before mitosis, the enzyme responsible for replication cuts off a section of the telomeres. Since this happens at a regular rate, telomeres can act as a sort of genetic clock, which forces the cell to die in a process called replicative senescence.

Elizabeth H. Blackburn, Jack W. Szostak, and Carol W. Greider shared this year’s prize for their combined efforts discovering and studying telomerase, an enzyme that freezes the telomeres’ genetic clocks by replacing lost DNA after replication. This research is important in the studies of aging and
cancer, which kills by mass and uncontrolled cell growth. Normally, telomerase is only active at the beginning of life; after it disappears from the cell the telomeres begin to shorten. Cancers reactivate the genes encoding telomerase, permitting the diseased cells to continue multiplying indefinitely. There are currently several clinical trials underway of cancer vaccines that act on telomerase to stop tumor growth.

Chemistry
The Central Dogma of molecular biology holds that protein production occurs in two stages: transcription of DNA’s genetic material into messenger RNA (mRNA) and translation of that mRNA into proteins. This second step has long been known to occur at the ribosome, which takes in mRNA and assembles amino acids into long, folded proteins.

Venkatraman Ramakrishnan of the MRC Laboratory of Molecular Biology in Cambridge, England; Thomas A. Steitz of Yale University; and Ada E. Yonath of the Weizmann Institute of Science in Rehovot, Israel won this year’s Nobel Prize in Chemistry for their work determining the precise structure and function of the ribosome. Yonath was cited in particular for developing a method of ribosomal crystallization, which enabled all three to develop a high-resolution model of the ribosome’s protein structure. Their work has been instrumental in the development of new antibiotics, according to the Swedish Academy of Sciences.

NICK WERLE B'10 is hoping that stress from his
thesis doesn’t give him dirty tail.