The intriguing crystal organization of the domain-swapped dimer of a human pancreatic ribonuclease variant indicates that the protein can form fibrils in solution. They were observed and characterized by atomic force microscopy. The importance of domain swapping in inducing native-like fibril formation is highlighted.

3D domain swapping and supramolecular protein assembly: insights from the X-ray structure of a dimeric swapped variant of human pancreatic RNase

PICA, ANDREA;MERLINO, ANTONELLO;PIZZO, ELIODORO;SICA, FILOMENA;
2013

Abstract

The intriguing crystal organization of the domain-swapped dimer of a human pancreatic ribonuclease variant indicates that the protein can form fibrils in solution. They were observed and characterized by atomic force microscopy. The importance of domain swapping in inducing native-like fibril formation is highlighted.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/562044
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