Pub. Date : 2010 Dec 17
PMID : 20947499
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Proline periodicity modulates the self-assembly properties of elastin-like polypeptides. | Proline | elastin | Homo sapiens |
| 2 | The monomeric precursor, tropoelastin, is highly hydrophobic yet remains substantially disordered and flexible in solution, due in large part to a high combined threshold of proline and glycine residues within hydrophobic sequences. | Proline | elastin | Homo sapiens |
| 3 | In fact, proline-poor elastin-like sequences are known to form amyloid-like fibrils, rich in beta-structure, from solution. | Proline | elastin | Homo sapiens |
| 4 | However, a small number of hydrophobic domains near the C terminus of tropoelastin are substantially depleted of proline residues. | Proline | elastin | Homo sapiens |
| 5 | Here we investigated the specific contribution of proline number and spacing to the structure and self-assembly propensities of elastin-like polypeptides. | Proline | elastin | Homo sapiens |
| 6 | These data strongly support a model where proline-poor regions of the elastin monomer provide a unique contribution to assembly and suggest a role for localized beta-sheet in mediating self-assembly interactions. | Proline | elastin | Homo sapiens |