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Proteins, Under Pressure!
Fundamental research conducted at Rensselaer on how proteins behave under high pressure is providing insights that could lead to novel engineering and biotechnology applications.
Shekhar Garde, assistant professor of chemical engineering, and his graduate student, Tuhin Ghosh, use molecular simulations to investigate effects of high pressure (~5,000 atmospheres) on protein structure and the interactions that drive the folding of proteins in water.
The structure of a protein swells in water but stays relatively compact when high pressure is applied. But researchers have not been able to understand why until recently.
A protein chain consists of two types of amino acidshydrophobic and hydrophilic. The hydrophobic particles repel water. In water-based solutions, they instinctively hide or fold inside the hydrophilic amino acids. The result is a unique 3-D structure for each kind of protein. The structure determines what a specific proteins function will be.
Molecular simulations in Gardes laboratory show that the key to pressure-induced swelling of proteins with water lies in the behavior of the water itself. With increasing pressure, water molecules are forced into the proteins hydrophobic interior, swelling the interior without greatly disrupting the overall conformation of the protein.
At higher pressures, the hydrogen-bonded water structure is crushed. As a result, attractions between hydrophobic amino acids are weakened. This destabilizes the folded structure of proteins but not enough to fully unfold them.
Gardes research could provide an understanding of how deep-sea organisms survive at high pressures. It could also help develop novel bioseparation methods in which pressure replaces harsh chemicals as a means to separate valuable proteins from complex mixtures.
The research, performed in collaboration with Angel E. Garcia at Los Alamos National Laboratory, was published in the Nov. 7 issue of the Journal of the American Chemical Society.
|Rensselaer Magazine: March 2002|
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