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20231223065649.0 |
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231223s2004 xx ||||| 00| ||eng c |
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|e rakwb
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|a eng
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| 100 |
1 |
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|a Sagis, Leonard M C
|e verfasserin
|4 aut
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| 245 |
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|a Mesoscopic properties of semiflexible amyloid fibrils
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| 264 |
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|c 2004
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| 336 |
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|a Text
|b txt
|2 rdacontent
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| 337 |
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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| 338 |
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|a Band
|b nc
|2 rdacarrier
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| 500 |
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|a Date Completed 03.02.2006
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|a Date Revised 26.10.2019
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|a published: Print
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|a Citation Status MEDLINE
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|a 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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|a Journal Article
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|a Amyloid
|2 NLM
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|a Lactoglobulins
|2 NLM
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|a Serum Albumin, Bovine
|2 NLM
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| 650 |
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|a 27432CM55Q
|2 NLM
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| 650 |
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|a Ovalbumin
|2 NLM
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| 650 |
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|a 9006-59-1
|2 NLM
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| 700 |
1 |
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|a Veerman, Cecile
|e verfasserin
|4 aut
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| 700 |
1 |
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|a van der Linden, Erik
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 20(2004), 3 vom: 03. Feb., Seite 924-7
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|x 1520-5827
|7 nnns
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|g volume:20
|g year:2004
|g number:3
|g day:03
|g month:02
|g pages:924-7
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