Determining exactly how proteins connect with specific DNA sequences in human cells has eluded researchers and scientists for years. While it has been possible to record the speed at which a protein could bond with DNA, little was known about how proteins located and connected with a specific pattern of DNA to allow genes to express themselves in the form of traits such as facial appearance, hair and eye color or behaviors.
In the July 16 issue of the journal Science, Rutgers-Newark chemistry professor Babis Kalodimos offers a solution to this puzzle in his paper, "Structure and Flexibility Adaptation in Nonspecific and Specific Protein-DNA Complexes." Kalodimos’ findings may be the clue researchers need to develop future methods to inhibit the expression of certain genes that may pre-dispose individuals to harmful diseases such as cancer and Alzheimer’s disease.
Through the use of the nuclear magnetic resonance (NMR) spectroscopy, Kalodimos and his co-workers were able to determine how proteins slide along the lengthy strands forming the helix structure of DNA until they reach their intended destination – a specific DNA sequence. More important, they illustrated in detail how proteins single out their partner DNA out of millions of non-functional ones.
Peter Haigney | EurekAlert!
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Physicists of the University of Würzburg have made an astonishing discovery in a specific type of topological insulators. The effect is due to the structure of the materials used. The researchers have now published their work in the journal Science.
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In experiments with magnetic atoms conducted at extremely low temperatures, scientists have demonstrated a unique phase of matter: The atoms form a new type of quantum liquid or quantum droplet state. These so called quantum droplets may preserve their form in absence of external confinement because of quantum effects. The joint team of experimental physicists from Innsbruck and theoretical physicists from Hannover report on their findings in the journal Physical Review X.
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