Capturing the Conformational Heterogeneity of HSPB1 Chaperone Oligomers at Atomic Resolution.

ABSTRACT: Small heat shock proteins (sHSPs), including HSPB1, are essential regulators of cellular proteostasis that interact with unfolded and partially folded proteins to prevent aberrant misfolding and aggregation. These proteins fulfill a similar role in biological condensates, where they interact with intrinsically disordered proteins to modulate their liquid-liquid and liquid-to-solid phase transitions. Characterizing the sHSP structure, dynamics, and client interactions is challenging due to their partially disordered nature, their tendency to form polydisperse oligomers, and their diverse range of clients. In this work, we leverage various biophysical methods, including fast ¹H-based magic angle spinning (MAS) NMR spectroscopy, molecular dynamics (MD) simulations, and modeling, to

SUBMITTER: Berkeley RF 

PROVIDER: S-EPMC12063158 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature