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| Home > Publications database > Features of Protein Unfolding Transitions and Their Relation to Domain Topology Probed by Single-Molecule FRET |
| Journal Article | FZJ-2023-05362 |
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2023
MDPI
Basel
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Please use a persistent id in citations: doi:10.3390/biom13091280 doi:10.34734/FZJ-2023-05362
Abstract: A protein fold is defined as a structural arrangement of a secondary structure in a threedimensionalspace. It would be interesting to know whether a particular fold can be assigned to certainfeatures of the corresponding folding/unfolding transitions. To understand the underlying principlesof the manifold folding transitions in more detail, single-molecule FRET is the method of choice.Taking the two-domain protein phosphoglycerate kinase (PGK) as an example, we investigateddenaturant-induced unfolded states of PGK using the above method. For this purpose, differentintramolecular distances within the two domains were measured. In addition to the known two-statetransition, a transition with a compact folding intermediate was also identified in each of the twodomains. Based on the structural homology of the domains (characterized by a Rossmann fold)and the striking similarity in the features of the measured distance changes during unfolding, clearevidence emerged that the underlying domain topology plays an important role in determining theobserved structural changes.
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