Characterization of refolded hen lysozyme variant lacking two outside disulfide bonds.
We characterized a refolded hen lysozyme variant containing only two SS-bonds, C64-C80 and C76-C94 (4CAHEL). From CD spectra and its activity, it was found that the refolded 4CAHEL has a structural topology analogous to wild-type lysozyme (WTHEL). Moreover, the refolded 4CAHEL showed no thermal transition, indicating that it had a character like a molten globule.
Ohkuri
Takatoshi
T
Graduate School of Pharmaceutical Sciences, Kyushu University, Maidashi, Fukuoka, Japan.
Imoto
Taiji
T
Ueda
Tadashi
T
D000818:Animals; D002645:Chickens; D009113:Muramidase / Q000737:chemistry*; D017510:Protein Folding
D009113:Muramidase