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, A., Merlino, A., A. K., B., T. J., K., Pizzo, E., G., D., Sica, F., L., M.. - In: ACTA CRYSTALLOGRAPHICA. SECTION D. - ISSN 1399-0047. - 69:10(2013), pp. 2116-2123. [10.1107/S0907444913020507]
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.| File | Dimensione | Formato | |
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