title: Analyses of native disulfide bond formations in the early stage of the folding process in mutant lysozymes where the long-range interactions in the denatured state were modulated.
abstract: In order to clarify whether modulation of long-range interactions in the denatured state affect native disulfide bond (SS bond) formations of hen egg white lysozyme (HEL) containing a pair of cysteine residues, we examined the extent of SS bond formation among 12 variants containing a pair of cysteines. The loss of clusters 5 and 6 in the denatured state affected the formation of Cys30-Cys115 and Cys6-Cys127 respectively.
authors: Graduate School of Pharmaceutical Sciences, Kyushu University, Maidashi, Fukuoka, Japan.
authors: Tomonori
authors: T
authors: Mishima
authors: Takatoshi
authors: T
authors: Ohkuri
authors: Taiji
authors: T
authors: Imoto
authors: Tadashi
authors: T
authors: Ueda
mesh_terms: D000818:Animals; D002645:Chickens; D004220:Disulfides / Q000737:chemistry; D004527:Egg Proteins; D009113:Muramidase / Q000737:chemistry* / Q000235:genetics; D009154:Mutation; D011489:Protein Denaturation; D017510:Protein Folding
chemical_list: D004220:Disulfides; D004527:Egg Proteins; D009113:Muramidase