Abstract
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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