Protein dynamics and interactions, in context
Most proteins adopt different structures to carry out their various biological functions. Intrinsically disordered proteins, or proteins that do not adopt a single, well-defined structure in isolation, represent a particularly interesting class of dynamic proteins, as they play critical roles in cellular signaling, regulation, and spatial organization. Intrinsically disordered proteins utilize dynamics and disorder to interact with and compete for molecular interaction partners in ways that are not possible for stably folded proteins and thus present many exciting avenues for future research.
Our Research Questions
What are the functional advantages of intrinsically disordered proteins?
How do disordered proteins enable cellular responses to stress in health and disease?
Can we develop new strategies to modulate the functions of dynamic molecules?
How do protein dynamics enable context-specific regulatory responses?
In the Berlow Lab, we use a highly interdisciplinary approach combining solution NMR spectroscopy, biophysics, structural biology, and complementary biological and chemical techniques to characterize disease-associated proteins that coordinate important cellular responses to molecular and environmental stress. A better understanding of how protein conformational states interconvert in different biological contexts will inform new strategies for selectively targeting disease-associated proteins.
