Introduction to Atomic Force Microscopy (AFM) in Biology
Open Access
- 15 November 2009
- journal article
- unit
- Published by Wiley in Current Protocols in Protein Science
- Vol. 58 (1) , 17.7.1-17.7.19
Abstract
The atomic force microscope (AFM) has the unique capability of imaging biological samples with molecular resolution in buffer solution. In addition to providing topographical images of surfaces with nanometer‐ to angstrom‐scale resolution, forces between single molecules and mechanical properties of biological samples can be investigated from the nanoscale to the microscale. Importantly, the measurements are made in buffer solutions, allowing biological samples to “stay alive” within a physiological‐like environment while temporal changes in structure are measured—e.g., before and after addition of chemical reagents. These qualities distinguish AFM from conventional imaging techniques of comparable resolution, e.g., electron microscopy (EM). This unit provides an introduction to AFM on biological systems and describes specific examples of AFM on proteins, cells, and tissues. The physical principles of the technique and methodological aspects of its practical use and applications are also described. Curr. Protoc. Protein Sci. 58:17.7.1‐17.7.19. © 2009 by John Wiley & Sons, Inc.Keywords
This publication has 99 references indexed in Scilit:
- Tensile Properties of Single Desmin Intermediate FilamentsBiophysical Journal, 2008
- Atomic Force Microscopy of Mammalian Urothelial SurfaceJournal of Molecular Biology, 2007
- Surface Tongue-and-groove Contours on Lens MIP Facilitate Cell-to-cell AdherenceJournal of Molecular Biology, 2000
- Watching amyloid fibrils grow by time-lapse atomic force microscopy 1 1Edited by W. BaumeisterJournal of Molecular Biology, 1999
- Surface analysis of the photosystem I complex by electron and atomic force microscopyJournal of Molecular Biology, 1998
- Growth of Protein 2-D Crystals on Supported Planar Lipid Bilayers Imagedin Situby AFMJournal of Structural Biology, 1998
- In situ observation of streptavidin‐biotin binding on an immunoassay well surface using an atomic force microscopeFEBS Letters, 1996
- Mechanical unfolding of a2‐macroglobulin molecules with atomic force microscopeFEBS Letters, 1996
- Atomic Force Microscopy of Cholera Toxin B-oligomers Bound to Bilayers of Biologically Relevant LipidsJournal of Molecular Biology, 1995
- Native Escherichia coli OmpF Porin Surfaces Probed by Atomic Force MicroscopyScience, 1995