The folding of hen lysozyme involves partially structured intermediates and multiple pathways.
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.
Radford
S E
SE
Oxford Centre for Molecular Sciences, University of Oxford, UK.
Dobson
C M
CM
Evans
P A
PA
D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D002942:Circular Dichroism; D005260:Female; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008958:Models, Molecular; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D013997:Time Factors
D009113:Muramidase