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Updated: Aug 15, 2026

Optimized Negative Staining: a High-throughput Protocol for Examining Small and Asymmetric Protein Structure by Electron Microscopy
Published on: August 15, 2014
[Structural changes of lipid and thyroxine-binding protein zones of lipoprotein particles, containing human
Abstract:
The relationship between temperature-induced structural changes in the lipid and protein thyroxine-binding zones of lipoprotein particles containing human apolipoprotein A-1 (apoA-1) as a sole protein component was studied using ESR with probes of two types--spin-labeled thyroxine and 5- or 16-doxylstearic acids. A structural rearrangement in the protein active site at 23-24 degrees was found. In the same temperature range, a dramatic change in the monolayer phospholipid ordered structure was observed. Based on these data, the localization of the apoA-1 thyroxine-binding site in the lipid phase as well as the possibility of regulation of the hormone binding process by changes in the protein-lipid interaction in lipoprotein particles are discussed.
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