Langmuir · 1996 · 123 citations · 19 references
Natural SciencesBiochemistryBiophysicsMolecular BiophysicsMolecular RecognitionSurface ScienceAtomic Force MicroscopyBiomolecular InteractionsBiomolecular InterfacesIntermolecular ForcesProtein AdsorptionScanning Probe MicroscopyAtomic Force Microscopy AnalysisAtomic Force Microscopy Surface AnalysisDivalent Ion EffectsReversible Affinity BindingSpecific AdsorptionTip-sample AdhesionTip-sample Interactions
Controlling DNA adsorption to atomically flat surfaces is crucial for studying protein−DNA interactions with the atomic force microscope (AFM). We present a method that enables reversible binding of this molecule to mica during AFM imaging in liquids. This can be acheived using a flow-through system which allows the exchange of different buffers that promote and inhibit the DNA adhesion to the surface. The DNA adsorption is controlled primarily through the divalent cation concentration. The DNA visibility in the AFM was investigated as a function of pH and cation concentration.
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Tapping mode atomic force microscopy in liquids
Paul K. Hansma, J. P. Cleveland, Manfred Radmacher et al. · Applied Physics Letters · 1994 · 868 citations
Forces in atomic force microscopy in air and water
A. L. Weisenhorn, Paul K. Hansma, T. R. Albrecht et al. · Applied Physics Letters · 1989 · 631 citations
The Schumann Resonance: A Global Tropical Thermometer
Earle Williams · Science · 1992 · 488 citations