Publications by authors named "Karina Guadalupe"
Structural biases in disordered proteins are prevalent in the cell.
Nat Struct Mol Biol
February 2024
Article Synopsis
- Intrinsically disordered proteins (IDPs) are important parts of cells that don’t fold into a specific shape like regular proteins do.
- IDPs can change their shape and have special interactions that help them work properly inside the cell.
- Research shows that the behavior of these proteins can change based on their environment and can be used for helpful purposes or in diseases.
Intrinsically disordered protein regions (IDRs) are ubiquitous across all kingdoms of life and play a variety of essential cellular roles. IDRs exist in a collection of structurally distinct conformers known as an ensemble. IDR amino acid sequence determines its ensemble, which in turn can play an important role in dictating molecular function.
View Article and Find Full Text PDFIntrinsically disordered protein regions (IDRs) are ubiquitous across all kingdoms of life and play a variety of essential cellular roles. IDRs exist in a collection of structurally distinct conformers known as an ensemble. An IDR's amino acid sequence determines its ensemble, which in turn can play an important role in dictating molecular function.
View Article and Find Full Text PDFCell homeostasis is perturbed when dramatic shifts in the external environment cause the physical-chemical properties inside the cell to change. Experimental approaches for dynamically monitoring these intracellular effects are currently lacking. Here, we leverage the environmental sensitivity and structural plasticity of intrinsically disordered protein regions (IDRs) to develop a FRET biosensor capable of monitoring rapid intracellular changes caused by osmotic stress.
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