Abstract
HS-AFM imaging is often performed to visualize dynamic processes of protein molecules during their functional activity. Therefore, we must be careful of the possible influences of tip–sample contact on the structure and the functional activity of the protein under study. Although the degree of this influence depends on the sample fragility, it is always good to know how large influences can occur quantitatively, depending on imaging conditions.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Fukuda, S., & Ando, T. (2021). Faster high-speed atomic force microscopy for imaging of biomolecular processes. Review of Scientific Instruments, 92, 033705.
Kodera, N., Sakashita, M., & Ando, T. (2006). Dynamic proportional-integral-differential controller for high-speed atomic force microscopy. Review of Scientific Instruments, 77, 083704.
Uchihashi, T., Iino, R., Ando, T., & Noji, H. (2011). High-speed atomic force microscopy reveals rotary catalysis of rotor-less F1-ATPase. Science, 333, 755–758.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
Copyright information
© 2022 Springer-Verlag GmbH Germany, part of Springer Nature
About this chapter
Cite this chapter
Ando, T. (2022). Influence of Tip–Sample Interactions on Specimens. In: High-Speed Atomic Force Microscopy in Biology. NanoScience and Technology. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-64785-1_7
Download citation
DOI: https://doi.org/10.1007/978-3-662-64785-1_7
Published:
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-662-64783-7
Online ISBN: 978-3-662-64785-1
eBook Packages: Chemistry and Materials ScienceChemistry and Material Science (R0)