Mesoscopic properties of semiflexible amyloid fibrils
We have determined the contour length, persistence length, bending rigidity, and critical percolation concentration for semiflexible amyloid fibrils formed from the globular proteins beta-lactoglobulin, bovine serum albumin, and ovalbumin. The persistence length was estimated using an adjusted rando...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 20(2004), 3 vom: 03. Feb., Seite 924-7 |
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| Format: | Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2004
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Amyloid Lactoglobulins Serum Albumin, Bovine 27432CM55Q Ovalbumin 9006-59-1 |
| Zusammenfassung: | We have determined the contour length, persistence length, bending rigidity, and critical percolation concentration for semiflexible amyloid fibrils formed from the globular proteins beta-lactoglobulin, bovine serum albumin, and ovalbumin. The persistence length was estimated using an adjusted random contact model for highly charged semiflexible chains. We have found contour lengths in the range of 50 nm to 10 microm and persistence lengths in the range of 16 nm to 1.6 microm. This wide range of contour and persistence lengths and the ease of preparation of these amyloid fibrils make them ideal model systems for the study of semiflexible polymers |
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| Beschreibung: | Date Completed 03.02.2006 Date Revised 26.10.2019 published: Print Citation Status MEDLINE |
| ISSN: | 1520-5827 |