Photo from wikipedia
Significance Protein aggregation is a major problem for human health. However, our understanding of how folded proteins aggregate into amyloid lags behind. Using the tripartite β-lactamase assay (TPBLA) with our… Click to show full abstract
Significance Protein aggregation is a major problem for human health. However, our understanding of how folded proteins aggregate into amyloid lags behind. Using the tripartite β-lactamase assay (TPBLA) with our test protein, β2-microglobulin (β2m), we show the ability to differentiate the behavior of single-point variants and highlight the remarkable sensitivity to the identity of the residue at position 76. After evolving the aggregation-prone protein, D76N-β2m, the only mutations able to improve D76N-β2m behavior in vivo involve residues in a single 7-residue sequence of the protein. Further characterization in vitro shows that a single-point mutant in this region can abolish D76N-β2m aggregation.
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Year Published: 2022
Link to full text (if available)
Share on Social Media: Sign Up to like & get
recommendations!