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Updated: May 26, 2026

Intracellular Refolding Assay
Published on: January 24, 2012
A mechanism of action for small heat shock proteins
1Department of Chemistry, St. Edward's University, Austin, TX 78704, USA. healy@stedwards.edu
Abstract:
Molecular dynamics simulations of a fitted multimeric structure of Mycobacterium tuberculosis α-crystallin (Mtb Acr) identify solvent exclusion from the β(4)-β(8) hydrophobic groove as a critical factor driving subunit assembly. Dehydration is also implicated as a determinant factor governing the chaperone activity of the dimer upon its dissociation from the oligomer. Two exposed hydrogen bonds, responsible for stabilizing the β(8)-β(9) fold are identified as key mechanistic elements in this process. Based on the overproduction of the chemokine CXCL16, observed after macrophage exposure to Mtb Acr, the proteases ADAM10 and ADAM17 are mooted as possible targets of this chaperone activity.
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