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Fredrik Höök

Researcher at Chalmers University of Technology

Publications -  233
Citations -  15888

Fredrik Höök is an academic researcher from Chalmers University of Technology. The author has contributed to research in topics: Lipid bilayer & Quartz crystal microbalance. The author has an hindex of 57, co-authored 220 publications receiving 14707 citations. Previous affiliations of Fredrik Höök include Lund University & Duke University.

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Characterization of DNA immobilization and subsequent hybridization on a 2D arrangement of streptavidin on a biotin-modified lipid bilayer supported on SiO2

TL;DR: It is demonstrated how this type of analysis can be used to control the state of streptavidin arrangement for improved measurements of DNA hybridization kinetics and a surface-coverage dependent viscoelastic behavior of immobilized b-DNA is shown to influence the hybridization efficiency.
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Bivalent Cholesterol-Based Coupling of Oligonucletides to Lipid Membrane Assemblies

TL;DR: Compared with DNA modified with one cholesterol moiety only, the binding strength to lipid membranes appears to be significantly stronger and even irreversible over the time scale investigated, which means that the bivalent coupling can be used to precisely control the number of DNA per lipid-membrane area.
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Simultaneous surface plasmon resonance and quartz crystal microbalance with dissipation monitoring measurements of biomolecular adsorption events involving structural transformations and variations in coupled water.

TL;DR: It is demonstrated for the first time, how the kinetics of the process during which adsorbed vesicles are spontaneously transformed into a supported phospholipid bilayer (SPB) on SiO(2) can be quantitatively separated into its two dominating states: adsor beds and supported planar bilayer patches.
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Label-Free Plasmonic Detection of Biomolecular Binding by a Single Gold Nanorod

TL;DR: Binding of streptavidin at 1 nM concentration induces a mean resonant wavelength shift of 0.59 nm suggesting that the current optical setup is able to reliably measure wavelength shifts as small as 0.3 nm, which is close to the limit of detection of the system.
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Localized surface plasmon resonance sensing of lipid-membrane-mediated biorecognition events.

TL;DR: The hole-induced localization of the LSPR field to the voids of the holes is demonstrated to provide an extension of theLSPR sensing concept to studies of reactions confined exclusively to SPB-patches supported on SiO2, and the possibility of performing label-free studies of lipid-membrane-mediated reaction kinetics is emphasized.