Spring Break
Biochemical Origami
Aggie scientists explore the world of protein folding and its significance
By: Nick Anthis
Issue date: 1/27/05 Section: Aggielife
The study by Sacchettini and Young demonstrates how protein folding can be unexpectedly complex.
Not a protein folding scientist by trade, Young studies bacteriophages (phages, for short), which are viruses acting as molecular parasites that infect bacterial cells.
Young says his work is important primarily because "it increases our understanding of how bacteriophages destroy bacterial cells." He said, "there is a coming medical revolution where bacteriophages are going to be used as medicines because we are running short on antibiotics" due to bacteria becoming increasingly resistant to them.
"(The phages') natural job is to destroy bacteria," Young said. "That's what they do for a living."
It may seem strange that phages would destroy their bacterial host, which they are completely dependent on, but after a phage infects a bacterial cell it reproduces itself rapidly, and its progeny must escape from their bacterial womb, killing the bacterial cell in the process.
A bacterial cell is protected by two layers: a weak and flexible membrane surrounded by a strong and rigid cell wall. The phage that Young studies uses the protein Lyz, a molecular time bomb that must not become active until needed, to break through the bacterial cell wall.
When phages produce Lyz inside of a bacterial cell, it accumulates in an inactive form in the bacterial membrane, due to the way it is folded.
When needed, Young said, Lyz "goes through a dramatic change in shape and changes its chemical bonding pattern." This new active form destroys the cell wall, releasing the imprisoned phages into a world ripe with new bacterial cells to attack.
"It's unprecedented for a protein to undergo this kind of change," Young said.
In addition to Young and Sacchettini, the other authors of this study are Min Xu, Arockiasamy Arulandu, Douglas Struck and Stephanie Swanson, an undergraduate student.
Sacchettini and his research group do not predict the shapes of proteins. They determine their actual structures using a process called X-ray crystallography. Arulandu, Swanson and Sacchettini determined the structures of the inactive and active forms of Lyz.
Not a protein folding scientist by trade, Young studies bacteriophages (phages, for short), which are viruses acting as molecular parasites that infect bacterial cells.
Young says his work is important primarily because "it increases our understanding of how bacteriophages destroy bacterial cells." He said, "there is a coming medical revolution where bacteriophages are going to be used as medicines because we are running short on antibiotics" due to bacteria becoming increasingly resistant to them.
"(The phages') natural job is to destroy bacteria," Young said. "That's what they do for a living."
It may seem strange that phages would destroy their bacterial host, which they are completely dependent on, but after a phage infects a bacterial cell it reproduces itself rapidly, and its progeny must escape from their bacterial womb, killing the bacterial cell in the process.
A bacterial cell is protected by two layers: a weak and flexible membrane surrounded by a strong and rigid cell wall. The phage that Young studies uses the protein Lyz, a molecular time bomb that must not become active until needed, to break through the bacterial cell wall.
When phages produce Lyz inside of a bacterial cell, it accumulates in an inactive form in the bacterial membrane, due to the way it is folded.
When needed, Young said, Lyz "goes through a dramatic change in shape and changes its chemical bonding pattern." This new active form destroys the cell wall, releasing the imprisoned phages into a world ripe with new bacterial cells to attack.
"It's unprecedented for a protein to undergo this kind of change," Young said.
In addition to Young and Sacchettini, the other authors of this study are Min Xu, Arockiasamy Arulandu, Douglas Struck and Stephanie Swanson, an undergraduate student.
Sacchettini and his research group do not predict the shapes of proteins. They determine their actual structures using a process called X-ray crystallography. Arulandu, Swanson and Sacchettini determined the structures of the inactive and active forms of Lyz.
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