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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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.
High resolution imaging of wheat and potato starch granule surfaces has been performed using low-voltage scanning electron microscopy and atomic force microscopy. The complimentary images of uncoated granules demonstrate that the two starch types possess substantially different surface topologies; potato starch has many protrusions (100-300 nm in diameter), above a flatter surface containing 20-50 nm structures, whilst wheat starch possesses far fewer protrusions and generally has a smoother surface composed of approximately 20 nm structures. The protrusions are believed to be carbohydrate in nature and thus represent the ends of amylopectin side-chain clusters at the granule surface.