Abstract
This chapter introduces atomic force microscopy (AFM) as an important tool for protein nanotechnology. A short review of AFM-based imaging, mapping, and spectroscopy of protein samples is given. AFM imaging of β-lactoglobulin nanofibrils in air is demonstrated. Basic concepts of AFM are described. Protocols for β-lactoglobulin nanofibrils and multiwall carbon nanotubes (MWCNT) samples preparation are defined. The operation of the microscope is described using MWCNT and the NanoScope E instrument in contact mode as an example. Nanostructure manipulation based on AFM nano-sweeping is demonstrated.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Similar content being viewed by others
References
MIAWiki page on interrelation between spectra, images and maps: http://confocal-manawatu.pbworks.com/w/page/16347061/Spectrum-Image-Map. Accessed 25 Dec 2011
Binnig G, Quate CF, Gerber C (1986) Atomic force microscope. Phys Rev Lett. doi:10.1103/PhysRevLett.56.930
Eaton P (2010) Atomic force microscopy. Oxford University Press, Oxford
Howland R, Benatar L, Symanski C (1998) A practical guide to scanning probe microscopy. DIANE publishing company, Darby
Morris VJ, Kirby AR, Gunning AP (2009) Atomic force microscopy for biologists. Imperial College Press, London
Li H, Oberhauser AF, Fowler SB et al (2000) Atomic force microscopy reveals the mechanical design of a modular protein. Proc Natl Acad Sci. doi:10.1073/pnas.120048697
Noy A, Frisbie CD, Rozsnyai LF et al (1995) Chemical force microscopy: exploiting chemically modified tips to quantify adhesion, friction, and functional group distributions in molecular assemblies. J Am Chem Soc. doi:10.1021/ja00135a012
Yu J, Bippes CA, Hand GM et al (2007) Aminosulfonate modulated pH-induced conformational changes in connexin26 hemichannels. J Biol Chem. doi:10.1074/jbc.M609317200
Stroh C, Wang H, Bash R et al (2004) Single-molecule recognition imaging microscopy. Proc Natl Acad Sci U S A. doi:10.1073/pnas.0403538101
Bash R, Wang H, Anderson C et al (2006) AFM imaging of protein movements: Histone H2A–H2B release during nucleosome remodelling. FEBS Lett. doi:10.1016/j.febslet.2006.06.101
Puech PH, Nevoltris D, Robert P et al (2011) Force measurements of TCR/pMHC recognition at T cell surface. PLoS One. doi:10.1371/journal.pone.0022344
Fuhrmann A, Ros R (2010) Single-molecule force spectroscopy: a method for quantitative analysis of ligand – receptor interactions. Nanomedicine. doi:10.2217/nnm.10.26
Rico F, Chu C, Moy VT (2011) Force-Clamp measurements of receptor–ligand interactions. In: Braga PC, Ricci D (eds) Atomic force microscopy in biomedical research: methods and protocols, methods in molecular biology. Humana Press, Totowa, NJ
Kuehner F, Costa LT, Bisch PM et al (2004) LexA-DNA bond strength by single molecule force spectroscopy. Biophys J. doi:10.1529/biophysj.104.048868
Rico F, Su C, Scheuring S (2011) Mechanical mapping of single membrane proteins at submolecular resolution. Nano Lett. doi:10.1021/nl202351t
Janovjak H, Kessler M, Oesterhelt D et al (2003) Unfolding pathways of native bacteriorhodopsin depend on temperature. EMBO J. doi:10.1093/emboj/cdg509
Rief M, Grubmüller H (2002) Force spectroscopy of single biomolecules. Chemphyschem. doi:10.1002/1439-7641(20020315)3:3<255::AID-CPHC255>3.0.CO;2-M
Kufer SK, Puchner EM, Gumpp H et al (2008) Single-molecule cut-and-paste surface assembly. Science. doi:10.1126/science.1151424
Kwon T, Park J, Yang J et al (2009) Nanomechanical in situ monitoring of proteolysis of peptide by Cathepsin B. PLoS One. doi:10.1371/journal.pone.0006248
Loveday SM, Wang XL, Rao MA et al (2010) Tuning the properties of β-lactoglobulin nanofibrils with pH, NaCl and CaCl2. Int Diary J. doi:10.1016/j.idairyj.2010.02.014
Bolder SG, Vasbinder AJ, Sagis LMC, van der Linden E (2007) Heat-induced whey protein isolate fibrils: conversion, hydrolysis, and disulphide bond formation. Int Diary J. doi:10.1016/j.idairyj.2006.10.002
Lapshin RV (2004) Feature-oriented scanning methodology for probe microscopy and nanotechnology. Nanotechnolgy. doi:10.1088/0957-4484/15/9/006
Sikora A, Sokolov DV, Danzebrink HU (2006) Scanning probe microscope setup with interferometric drift compensation. In: Wilkening G, Koenders L (eds) Nanoscale calibration standards and methods: dimensional and related measurements in the micro- and nanometer range. Wiley, Weinheim
Acknowledgements
The author would like to thank Professor Richard Haverkamp, School of Engineering and Advanced Technology, and Dr. Mark Waterland, Institute for Fundamental Sciences, Massey University, for their support and opportunity to work with scanning probe microscopes. The author would also like to thank Dr. Mark Patchett, Institute of Molecular BioSciences, for his valuable suggestions, and Dr. Simon Loveday, Riddet Institute, and Mike Seawright, Institute for Fundamental Sciences, Massey University, for supplying protein and nanotubes samples and technical assistance with sample preparation for AFM.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2013 Springer Science+Business Media, New York
About this protocol
Cite this protocol
Sokolov, D.V. (2013). Atomic Force Microscopy for Protein Nanotechnology. In: Gerrard, J. (eds) Protein Nanotechnology. Methods in Molecular Biology, vol 996. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-354-1_19
Download citation
DOI: https://doi.org/10.1007/978-1-62703-354-1_19
Published:
Publisher Name: Humana Press, Totowa, NJ
Print ISBN: 978-1-62703-353-4
Online ISBN: 978-1-62703-354-1
eBook Packages: Springer Protocols