Báo cáo khoa học: Substitution of residues at the double dimer interface affects the stability and oligomerization of goose d-crystallin
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d-Crystallin is the major structural protein in avian and reptilian eye lenses,and confers special refractive properties. The protein is a homotetramerarranged as a dimer of dimers. In the present study, the roles of the sidechains of Glu267, Lys315, and Glu327, which provide hydrogen bonds atthe double dimer interface, were investigated. Hydrophobic side chain sub-stitution led to all mutant proteins having an unstable dimer interface.
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: Substitution of residues at the double dimer interface affects the stability and oligomerization of goose d-crystallin
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: Substitution of residues at the double dimer interface affects the stability and oligomerization of goose d-crystallin
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