Author: Maria Temming / Source: Science News for Students
Biologists often refer to evolution as the way living things adapt, genetically, to their environment.
But scientists sometimes harness “evolution” to help out in other fields of science. Three who did were today awarded the 2018 Nobel Prize in chemistry. They developed ways to build proteins in the lab through the use of evolution.The proteins that can be fashioned this way are suitable for a broad range of uses. These range from new drugs to biofuels.
Frances Arnold works at the California Institute of Technology in Pasadena. She will take home half of this year’s prize of 9 million Swedish kronor (about $1 million). She worked on enzymes. These are materials that cells create to speed up chemical reactions. Arnold learned how to make new enzymes from old ones. These new enzymes can be used to make biofuels, environmentally friendly detergents and other products.
Arnold is only the fifth woman over the past 117 years to win a Nobel Prize in chemistry.
Gregory Winter works in England at the University of Cambridge. George Smith is at the University of Missouri in Columbia. They will split the other half of this year’s chemistry prize. They found a way to build peptides (short strings of amino acids) using viruses. Some of the peptides are used to make antibodies and other medicines.
“Wow, well-deserved!” says Paul Dalby of this year’s prize winners. “Protein engineering as a field is absolutely founded upon their work,” he notes. Dalby is a biochemical engineer. He works in England at University College London.
All three winners will collect a medal and their shares of the prize money at a ceremony in Stockholm, Sweden on December 10. That’s the date in 1896 on which Alfred Nobel died.
Mining the chemical know-how of living organisms
In the late 1980s, Arnold wanted to make an enzyme to break down a milk protein, casein, in a solvent other than water. She could try to manually link up the amino-acid building blocks of that enzyme to give it the right properties. That would require knowing which amino acids to change. Instead, she opted for a more hands-off approach.
Arnold’s insight, says Jesse Bloom, “was to recognize that the most amazing molecules in the world weren’t created by chemists.” He is a microbiologist at the Fred Hutchinson Cancer Research Center in Seattle, Wash. Those cool molecules are made in the cells of living things. What’s more, he notes, “Biology didn’t make these chemicals using the methods we might learn in an organic chemistry class. Rather, it worked by evolution.”
Arnold first made many copies of the DNA that contains instructions for making the original enzyme. She put that DNA into bacteria. As the bacteria grew, genetic differences — changes known as mutations — arose by accident.
Each batch of bacteria could have many different versions of the mutant enzyme-making genes. The bacteria also acted like living factories. They churned out many copies of each mutant enzyme. Arnold picked the version of that enzyme that did the best job at breaking down casein in a particular solvent. Then she repeated the mutation process, starting the best-working enzyme.
Her bacteria went through rounds of mutation-making. Each time she selected the best-working enzyme that some…
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