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From Native to Non-Native Two-Dimensional Protein Lattices through Underlying Hydrophilic/Hydrophobic Nanoprotrusions

Authors


  • S.M.-F. thanks the Max-Planck-Gesellschaft for financial support and acknowledges Rüdiger Berger and Prof. Wolfgang Knoll for the AFM&SPR facilities. J.L.T.-H. thanks the Ramón y Cajal program of the Spanish government. The authors are grateful to Jacqueline Friedmann for technical support on S-proteins and Kathryn Melzak, Radostina Georgieva, and Paula Pescador for useful comments. We are indebted to the Deutsche Forschungsgemeinschaft for support on the synthetic work. This work has been additionally supported by the US Air Force Office of Scientific Research (project nos.: FA9550-06-0208 and FA9550-07-1-0313) and the Spanish Government (grant no.: CTQ2007-66541).

Abstract

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Tuning to the terminals: Controlled tuning of protein–substrate interactions induces a transition from native to non-native protein crystals (see AFM images) as—depending on m, the chain-length difference, which determines whether surface protrusions are hydroxy or methyl functionalized—the underlying non-ion-mediated interactions are gradually transformed from mainly associative (H-bonding) to hydrophobic.

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