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Investigation of Protein Structure at the Solid/Liquid Interface with Atomic Force Microscopy (Afm)

Published online by Cambridge University Press:  02 July 2020

M.J. Waner ,
M. Schindler  and
M. Dantus
M.J. Waner
Affiliation:
Department of Chemistry, Michigan State University, East Lansing, MI48824
M. Schindler
Affiliation:
Department of Biochemistry, Michigan State University, East Lansing, MI48824
M. Dantus
Affiliation:
Department of Chemistry, Michigan State University, East Lansing, MI48824
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Extract

At present, changes in the structure of proteins occurring upon adsorption at liquid/solid interfaces are not well understood. The prevailing model assumes that a protein, which is globular in solution, must first displace surface bound water molecules. Then, after adsorption of the protein at the surface, the molecule unfolds to maximize interactions with the surface. It is noted, however, that some enzymes maintain a significant amount of their activity once adsorbed. This observation is the basis for many biomedical assays and implies that native protein structure is at least partially maintained.

The atomic force microscope (AFM) is well suited for the study of biomolecules at interfaces, providing single molecule resolution. Progress on molecular structure analysis of proteins using AFM, however, has been hampered by the fact that the tip radius is as large as, or larger than the proteins themselves, thereby causing a large lateral convolution effect.

Type
Scanned Probe Microscopies: Technologies, Methodologies, and Applications
Information
Microscopy and Microanalysis , Volume 3 , Issue S2: Proceedings: Microscopy & Microanalysis '97, Microscopy Society of America 55th Annual Meeting, Microbeam Analysis Society 31st Annual Meeting, Histochemical Society 48th Annual Meeting, Cleveland, Ohio, August 10-14, 1997 , August 1997 , pp. 1257 - 1258
Copyright
Copyright © Microscopy Society of America 1997

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References

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