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Updated: Jul 5, 2026

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
Published on: May 29, 2011
[Changes in the model membrane structure induced by ribonuclease and lysozyme studied by the fluorescent probe
1Kharkov State University, Ukraine.
Abstract:
Using fluorescent probes DSM and DSP-12, the effect of ribonuclease and lysozyme on the structural state of liposomes composed of phosphatidylcholine and diphosphatidylglycerol was studied. A correlation between the changes in probe quantum yield and the amount of protein-bound lipids was established. It is assumed that the formation of protein-lipid complexes increases the packing density of lipids and restricts their mobility. As the content of diphosphatidylglycerol in the lipid bilayer increases, the condensing effect of proteins becomes more pronounced.
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