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- W2898814996 abstract "Abstract Theory and simulations predicted sometime ago that the sizes of unfolded states of globular proteins should decrease continuously as the denaturant concentration is shifted from a high to a low value. However, small angle X-ray scattering (SAXS) data were used to assert the opposite, while interpretation of single molecule Forster resonance energy transfer experiments (FRET) supported the theoretical predictions. The disagreement between the two experiments is the SAXS-FRET controversy. By harnessing recent advances in SAXS and FRET experiments and setting these findings in the context of a general theory and simulations, we establish that compaction of unfolded states is universal. The theory also predicts that proteins rich in β -sheets are more collapsible than α -helical proteins. Because the extent of compaction is small, experiments have to be accurate and their interpretations should be as model free as possible. Theory also suggests that collapsibility itself could be a physical restriction on the evolution of foldable sequences, and provides a physical basis for the origin of multi-domain proteins." @default.
- W2898814996 created "2018-11-09" @default.
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- W2898814996 date "2018-11-02" @default.
- W2898814996 modified "2023-10-16" @default.
- W2898814996 title "Universal nature of collapsibility in the context of protein folding and evolution" @default.
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- W2898814996 doi "https://doi.org/10.1101/461046" @default.
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