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Unfolding the Mystery of Transformer-like Proteins

Lauren Porter’s Research on Fold-switching Proteins

May 06, 2022

From the NIH Catalyst by Natalie Hagan, NCATS

For decades it was thought that when proteins fold, they assume only one stable structure that performs a specific function. For example, the unique structure of the protein hemoglobin allows it to transport oxygen from the lungs to the tissues. This one-sequence-one-fold paradigm is attributed to NIH’s Christian Anfinsen, who won the 1972 Nobel Prize in Chemistry. His work established a connection between the amino acid sequence that makes up a protein and its three-dimensional shape, or conformation, that dictates the protein’s biological function.

Stadtman Tenure-Track Investigator Lauren Porter’s research on fold-switching proteins challenges the ubiquity of this one-sequence-one-structure paradigm. “Fold-switching proteins are like Transformers, like Optimus Prime,” said Porter, referring to the hero of the science fiction franchise of shapeshifting humanlike robots. “Sometimes he’s a robot, and sometimes he turns into a car. He uses both of his structures and both of his functions to fight crime.” Similarly, the proteins she studies have multiple stable structures and functions.

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