FEBS Letters · 1996 · 132 citations · 15 references
Natural SciencesBiochemistryBiophysicsBiophysical ChemistryMolecular BiophysicsStructural BiologyAtomic Force MicroscopyGlobular ProteinsIntermolecular ForcesMacromolecular StructureProtein DynamicsProtein StructureAtomic Force Microscopy AnalysisForce MeasurementForce-dependent Protein UnfoldingMechanical Unfolding PathwaysNoncontact Atomic Force MicroscopyProtein Unfolding KineticsProtein-surface InteractionsUnfolding Kinetics
alpha2-Macroglobulin was derivatized with a sulfhydryl cross-linker and sandwiched between a mica substrate and a silicon nitride tip, both coated with gold, of an atomic force microscope and force curve measurement was carried out. An extensive downward deflection of the cantilever was observed in the retracting realm of the curve, when and only when the substrate was covered with the derivatized protein. The result was interpreted in terms of the mechanical stretching and unfolding of a single or a few protein molecules.
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