Abstract
Analysis of the folding of hen lysozyme shows that the protein does not become organized in a single cooperative event but that different parts of the structure become stabilized with very different kinetics. In particular, in most molecules the α-helical domain folds faster than the β-sheet domain. Furthermore, different populations of molecules fold by kinetically distinct pathways. Thus, folding is not a simple sequential assembly process but involves parallel alternative pathways, some of which may involve substantial reorganization steps.
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Radford, S., Dobson, C. & Evans, P. The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature 358, 302–307 (1992). https://doi.org/10.1038/358302a0
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DOI: https://doi.org/10.1038/358302a0
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