The Protein Folding Problem - dasher wustl 2025

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The 2024 Nobel Prize in chemistry recognized Demis Hassabis, John Jumper and David Baker for using machine learning to tackle one of biologys biggest challenges: predicting the 3D shape of proteins and designing them from scratch.
On average, AlphaFold2 successfully predicted the 3D structure of proteins within the width of about one atom, leading the CASP organizers to declare the protein folding problem solved [11].
David Baker. (Image by University of Washington.) The scientist awarded the 2024 Nobel Prize in Chemistry for using computer software to invent a new protein used supercomputers and ultrabright X-rays at two facilities located at the U.S. Department of Energys (DOE) Argonne National Laboratory.
In the 1960s, Christian Anfinsen, PhD 43, proved that the sequence of these amino acids is like a recipe for how the protein will shift into its ultimate shape. It starts as a floppy kind of spaghetti floating in water, Bouatta says. Then it starts folding.
In 2020, John Jumper and Demis Hassabis presented an AI model called AlphaFold2. With its help, they have been able to predict the structure of virtually all known proteins. AlphaFold2 has been widely used in many areas, including research into pharmaceuticals and environmental technology.
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The paradox involves the observation that there is insufficient time to randomly search the entire conformational space available to a polypeptide chain as an unfolded protein (Levinthal, 1968). The obvious resolution, and this was Levinthals point, is that proteins have to fold through some directed process.
The 2024 chemistry Nobel was awarded to John Jumper and Demis Hassabis at Google DeepMind in London, for developing a game-changing AI tool for predicting protein structures called AlphaFold, and David Baker, at the University of Washington in Seattle, for his work on computational protein design, which has been

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