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 scene is all too familiar. A parent opens the door to a messy room with clothes strewn about and yells at the sulking teen, "Clean up your room ... and fold up those clothes!" Understandably, the teen is not very motivated by such a mundane task.
In fact, we rarely give folding more than a second thought. At the microscopic level, though, folding takes on a whole new meaning. A team of A&M scientists, led by biochemistry professors James Sacchettini and Ry Young, report on a protein that can transform from a molecular bystander to a chemical bulldozer by changing the way it is folded. Their results were published in the Jan. 7 issue of the journal Science.
Our bodies are made up of different types of cells, which are themselves made up of different types of molecules. Some of the molecules, called proteins, are linear chains of different chemical blocks called amino acids and the true workhorses of the biochemical world.
A snake-like chain of amino acids without a distinct shape is virtually useless. Therefore, a protein must fold into a varying three-dimensional shape to function properly. This holds true in all life forms, from complex humans to bacteria made of only one tiny cell.
Nick Pace, professor of biochemistry at A&M, studies protein folding. He is one of many scientists trying to solve the "protein folding problem."
"Protein folding means being able to predict the three-dimensional structure of a protein," Pace said.
Correct folding is important, Pace said, because "many diseases are protein folding diseases," including Alzheimer's disease, Huntington's disease and cystic fibrosis. In these diseases, incorrect folding of important proteins causes the disease's symptoms.
Think of protein folding as biochemical origami - a bland chemical chain masterfully folded into an elegant and efficient protein machine.
Theoretically, the specific order of amino acids should determine the three-dimensional shape of the protein, just like a sheet of paper able to fold itself into an elegant origami swan.
In fact, we rarely give folding more than a second thought. At the microscopic level, though, folding takes on a whole new meaning. A team of A&M scientists, led by biochemistry professors James Sacchettini and Ry Young, report on a protein that can transform from a molecular bystander to a chemical bulldozer by changing the way it is folded. Their results were published in the Jan. 7 issue of the journal Science.
Our bodies are made up of different types of cells, which are themselves made up of different types of molecules. Some of the molecules, called proteins, are linear chains of different chemical blocks called amino acids and the true workhorses of the biochemical world.
A snake-like chain of amino acids without a distinct shape is virtually useless. Therefore, a protein must fold into a varying three-dimensional shape to function properly. This holds true in all life forms, from complex humans to bacteria made of only one tiny cell.
Nick Pace, professor of biochemistry at A&M, studies protein folding. He is one of many scientists trying to solve the "protein folding problem."
"Protein folding means being able to predict the three-dimensional structure of a protein," Pace said.
Correct folding is important, Pace said, because "many diseases are protein folding diseases," including Alzheimer's disease, Huntington's disease and cystic fibrosis. In these diseases, incorrect folding of important proteins causes the disease's symptoms.
Think of protein folding as biochemical origami - a bland chemical chain masterfully folded into an elegant and efficient protein machine.
Theoretically, the specific order of amino acids should determine the three-dimensional shape of the protein, just like a sheet of paper able to fold itself into an elegant origami swan.
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