TY  - JOUR
AU  - Bustorff, Nuno
AU  - Fitter, Jörg
TI  - Features of Protein Unfolding Transitions and Their Relation to Domain Topology Probed by Single-Molecule FRET
JO  - Biomolecules
VL  - 13
IS  - 9
SN  - 2218-273X
CY  - Basel
PB  - MDPI
M1  - FZJ-2023-05362
SP  - 1280 -
PY  - 2023
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - 37759680
UR  - <Go to ISI:>//WOS:001074347000001
DO  - DOI:10.3390/biom13091280
UR  - https://juser.fz-juelich.de/record/1019402
ER  -