NBS-nytt
25.11.2018
This year's Nobel Prize in Chemistry has been awarded to Frances H. Arnold (50 %), George P. Smith (25 %) and Sir Gregory P. Winter (25 %). The laureates have pioneered laboratory evolution of proteins, one of the great scientific and biotechnological advances of the past three decades.
Through billions of years, natural evolution has created a phenomenal biodiversity. One example of this diversity is that living organisms produce a wide variety of natural enzymes that catalyze a plethora of chemical reactions, under all kinds of conditions, with exquisite specificity and efficiency. As another example of Nature's evolvability and adaptability, living organisms exploit evolutionary power also in their daily life, one prime example being the recombination mechanisms that are at the basis of mammalian immune systems and that enable rapid and specific antibody responses to pathogens. The 2018 Nobel Laureates in Chemistry have brought evolution to lab. They have developed and used methods to control and “direct" evolution, and they have used their tools to develop enzymes and antibodies for the benefit to humankind.
Frances Arnold was one of the first to realize that the evolution in Nature could be captured in the laboratory. In a time where “protein engineering" was one of the hot topics in biochemistry and PCR was still relatively new, she realized that instead of trying to improve proteins by introducing single, designed mutations, one at the time, one could rather produce libraries of more randomly generated mutants and screen these for variants with desired properties. At the time, Arnold was interested in making enzymes work in organic solvents and in 1993 she published a breakthrough paper entitled “Tuning the activity of an enzyme for unusual environments: sequential random mutagenesis of sub
Gå til medietFrances Arnold was one of the first to realize that the evolution in Nature could be captured in the laboratory. In a time where “protein engineering" was one of the hot topics in biochemistry and PCR was still relatively new, she realized that instead of trying to improve proteins by introducing single, designed mutations, one at the time, one could rather produce libraries of more randomly generated mutants and screen these for variants with desired properties. At the time, Arnold was interested in making enzymes work in organic solvents and in 1993 she published a breakthrough paper entitled “Tuning the activity of an enzyme for unusual environments: sequential random mutagenesis of sub