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- W2012164642 abstract "Cooperative protein folding invokes discrete folded and unfolded ensembles separated by a free-energy barrier. In contrast, downhill folding involves just one ensemble of protein molecules within a single free-energy well. Common method of monitoring the folding transition which yield mean values cannot resolve the two mechanisms. Time-resolved dynamic resonance nonradiative excitation energy transfer (trFRET), which can yield distributions of conformers in ensembles of partially folded protein molecules was applied. E. Coli adenylate kinase (AK) was used as a model in a study of the unfolding/refolding transition. Several mutants were prepared which enabled monitoring the folding transition at different parts of the molecule.The analysis of trFRET monitored chemically induced unfolding/refolding transition yielded a clear evidence for the presence of two distinct sub-populations at the transition zone. One sub-population was native like and the other was unfolded. The proportion of the size of the two sub-populations was varied as function of the concentration of the denaturant.These experiments yielded solid evidence in support the model of cooperative, barrier crossing, mechanism of folding this protein. At least for this case, the model of downhill mechanism of folding is not applicable." @default.
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- W2012164642 date "2009-02-01" @default.
- W2012164642 modified "2023-09-29" @default.
- W2012164642 title "Time-resolved Fret Study Shows Sub-populations of A Globular Protein Molecules at The Refolding Transition Zone" @default.
- W2012164642 doi "https://doi.org/10.1016/j.bpj.2008.12.2905" @default.
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