PubMed · 8840802
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K Amako, A Umeda. 1996. [Scanning probe microscope].. https://pubmed.ncbi.nlm.nih.gov/8840802/
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Atomic force microscopes (AFMs) move a sharp tip attached to a soft cantilever in a TV-raster-like pattern over a surface and record deflections of the tip that correspond to the surface topography. When operated in physiological solutions, an AFM allows biomolecules to be observed in their native environment. Progress in instrumentation, sample-preparation methods and recording conditions has provided images of biomolecules and their assemblies that reveal submolecular details. In addition, the AFM allows conformational changes to be observed directly. This article discusses these points and illustrates them with some pertinent examples.
Biological atomic force microscopy (AFM) is now established as a method for studying the structure and function of biomolecular objects at the solid-liquid interface. Major progress in this field is linked to new developments in instrumentation, a better understanding of tip-sample interactions, and improved sample preparation techniques. In this review, the most common strategies for biomolecular immobilization with respect to biological AFM applications are summarized.
Atomic force microscopy (AFM) was applied to study uncoated virus particles and RNA prepared by stripping of tobacco mosaic virions (TMV) with mild alkali or urea and dimethylsulfoxide. We found that AFM is an appropriate method to study ribonucleoprotein and free RNA structures. Images of entire tobacco mosaic virions, partially uncoated TMV particles with protruding RNA molecule from one or both ends and individual RNA molecules are presented.