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Molecular organization of amyloid protofilament-like assembly of betabellin 15D: helical array of beta-sandwiches.
Betabellin is a 32-residue peptide engineered to fold into a four-stranded antiparallel beta-sheet protein. Upon air oxidation, the betabellin peptides can fold and assemble into a disulfide-bridged homodimer, or beta-sandwich, of 64 residues. Recent biophysical and ultrastructural studies indicate...
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| Main Authors: | , , , , , |
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| Format: | Artigo |
| Sprog: | English |
| Udgivet: |
2002
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1302267/ https://ncbi.nlm.nih.gov/pubmed/12202394 |
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