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.
authors.affiliation: IMETUM, Physics Department, CeNS and CIPSM, Technische Universität München, 85748 Garching, Germany.
authors.forename: Michael
authors.initials: M
authors.lastname: Geisler
authors.forename: Senbo
authors.initials: S
authors.lastname: Xiao
authors.forename: Elias M
authors.initials: EM
authors.lastname: Puchner
authors.forename: Frauke
authors.initials: F
authors.lastname: Gräter
authors.forename: Thorsten
authors.initials: T
authors.lastname: Hugel
mesh_terms: D005349:Fibroins / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D056004:Molecular Dynamics Simulation; D010446:Peptide Fragments / Q000737:chemistry; D017433:Protein Structure, Secondary; D013499:Surface Properties; D013816:Thermodynamics
chemical_list: D010446:Peptide Fragments; D005349:Fibroins