Controlling the structure of proteins at surfaces
With the help of single molecule force spectroscopy and molecular dynamics simulations, we determine the surface-induced structure of a single engineered spider silk protein. An amyloid like structure is induced in the vicinity of a surface with high surface energy and can be prohibited in the prese...
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| Main Authors: | , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
August 20, 2010
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| In: |
Journal of the American Chemical Society
Year: 2010, Volume: 132, Issue: 48, Pages: 17277-17281 |
| ISSN: | 1520-5126 |
| DOI: | 10.1021/ja107212z |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1021/ja107212z
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| Author Notes: | Michael Geisler, Senbo Xiao, Elias M. Puchner, Frauke Gräter, and Thorsten Hugel |
| Summary: | With the help of single molecule force spectroscopy and molecular dynamics simulations, we determine the surface-induced structure of a single engineered spider silk protein. An amyloid like structure is induced in the vicinity of a surface with high surface energy and can be prohibited in the presence of a hydrophobic surface. The derived molecular energy landscapes highlight the role of single silk protein structure for the macroscopic toughness of spider silk. |
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| Item Description: | Gesehen am 24.02.2023 |
| Physical Description: | Online Resource |
| ISSN: | 1520-5126 |
| DOI: | 10.1021/ja107212z |