Structural studies of three-dimensional domain swapping and amyloid formation.
- Resource Type
- Theses
- Authors
- Liu, Yanshun
- Source
- Dissertation Abstracts International; Dissertation Abstract International; 62-08B.
- Subject
- Chemistry, Biochemistry
- Language
- English
Summary: To test the 3D domain-swapping zipper model for amyloid formation, we inserted poly-glutamine, poly-asparagine and prion peptide from the yeast prion Sup35 into the hinge loops of RNase A. The RNase A mutants spontaneously dimerize under native conditions, whereas dimerization of the wild type RNase A requires acidic conditions. Fiber formation of some mutants is also related to the length of the hinge loop. These results are consistent with the 3D domain-swapping zipper model. They also shed some light onto the mechanism of 3D domain swapping.