Controlling the structure of proteins at surfaces

Michael Geisler; Senbo Xiao; Elias M. Puchner; Frauke Gräter; Thorsten Hugel

doi:10.1021/ja107212z

Controlling the structure of proteins at surfaces

Michael Geisler, Senbo Xiao, Elias M. Puchner, Frauke Gräter, Thorsten Hugel

Physics and Astronomy (Twin Cities)

Research output: Contribution to journal › Article › peer-review

17 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	17277-17281
Number of pages	5
Journal	Journal of the American Chemical Society
Volume	132
Issue number	48
DOIs	https://doi.org/10.1021/ja107212z
State	Published - Dec 8 2010

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title = "Controlling the structure of proteins at surfaces",

abstract = "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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AU - Geisler, Michael

AU - Xiao, Senbo

AU - Puchner, Elias M.

AU - Gräter, Frauke

AU - Hugel, Thorsten

PY - 2010/12/8

Y1 - 2010/12/8

N2 - 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.

AB - 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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Controlling the structure of proteins at surfaces

Abstract

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