Kinetic refolding barrier of guanidinium chloride denatured goose delta-crystallin leads to regular aggregate formation.

ABSTRACT: Delta-crystallin is the major soluble protein in avian eye lenses with a structural role in light scattering. Dissociation and unfolding of the tetrameric protein in guanidinium chloride (GdmCl) can be sensitively monitored by the intrinsic tryptophan fluorescence. In this study refolding of GdmCl-denatured delta-crystallin was investigated. A marked hysteresis was observed while refolding by dilution of the 5 M GdmCl-denatured delta-crystallin. The secondary structure of the refolded protein was largely restored. However, monitoring intrinsic fluorescence of single tryptophan mutants indicated that the microenvironment of domain 1 (W74) was not restored. The region containing W169, which is close to the dimer interface, remained exposed following refolding. During refolding of the wild-ty

SUBMITTER: Yin FY 

PROVIDER: S-EPMC1929020 | biostudies-literature | 2007 Aug

REPOSITORIES: biostudies-literature