Frederick Lab

UT Southwestern Medical Center

BIOCHEMISTRY

Dallas · United States

NIH-funded
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NIH R01 · 2024

High sensitivity NMR for structure determination of neurodegenerative disease associated protein aggregates in native contexts

For an organism to survive, its proteins must adopt a diversity of conformations in a challenging environment where macromolecular crowding can derail even robust biological pathways. This situation becomes critical when considering proteins with energetic folding landscapes that permit many conformational states. In these cases, the environment can clearly influence the conformation by favoring one pathway over another. Because the aggregating proteins that are responsible for neurodegenerative diseases like Alzheimer’s and Parkinson’s diseases often have identical sequences in healthy and diseased individuals, differences in cellular environment are responsible for the conformational…

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