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- W2170531080 abstract "Individual Concanavalin A (ConA) molecules have been imaged at the liquid/solid interface with an atomic force microscope (AFM). Three-dimensional sizing with very high resolution (<5 Å) has been obtained by a novel approach based on height distributions, which avoids the tip convolution effects which normally affect scanning probe microscopy techniques. Each height measurement correlates to a particular molecular orientation on the surface. A large number of such measurements provide a statistical ensemble of orientations. The complete height distribution reflects the three-dimensional size of the protein sample and hence its tertiary and quaternary structure. A surface adsorption and orientation model, based on a minimization of surface adsorption energy, is proposed. This model is in good agreement with the observed height distribution of Con A molecules at the liquid/solid interface. Analysis of Con A and succinylated Con A molecules on mica demonstrates that Con A dimers are the prevalent species at the liquid/solid interface. This is in contrast to the tetrameric organization of Con A normally observed in solution. The new possibilities opened by height distribution analysis on the physical characterization of biomolecules at interfaces are also discussed." @default.
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- W2170531080 date "1998-02-04" @default.
- W2170531080 modified "2023-10-06" @default.
- W2170531080 title "Imaging the Molecular Dimensions and Oligomerization of Proteins at Liquid/Solid Interfaces" @default.
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- W2170531080 doi "https://doi.org/10.1021/jp9732219" @default.
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