The folding of hen lysozyme involves partially structured intermediates and multiple pathways.

S E Radford; C M Dobson; P A Evans

doi:10.1038/358302a0

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The folding of hen lysozyme involves partially structured intermediates and multiple pathways.

S E Radford·C M Dobson·P A Evans

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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 alpha-helical domain folds faster than the beta-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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Amino Acid Sequence Animals Chickens Circular Dichroism Female Hydrogen-Ion Concentration Kinetics Models, Molecular Muramidase Protein Conformation Time Factors Journal Article Research Support, Non-U.S. Gov't

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S E Radford, C M Dobson, P A Evans. 1992-07-23. The folding of hen lysozyme involves partially structured intermediates and multiple pathways.. https://doi.org/10.1038/358302a0

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