Atomic force microscopy of biological membranes.
Atomic force microscopy (AFM) is an ideal method to study the surface topography of biological membranes. It allows membranes that are adsorbed to flat solid supports to be raster-scanned in physiological solutions with an atomically sharp tip. Therefore, AFM is capable of observing biological molecular machines at work. In addition, the tip can be tethered to the end of a single membrane protein, and forces acting on the tip upon its retraction indicate barriers that occur during the process of protein unfolding. Here we discuss the fundamental limitations of AFM determined by the properties of cantilevers, present aspects of sample preparation, and review results achieved on reconstituted and native biological membranes.
Frederix
Patrick L T M
PL
M. E. Müller Institute for Structural Biology, Biozentrum, University of Basel, Basel, Switzerland.
Bosshart
Patrick D
PD
Engel
Andreas
A
D000465:Algorithms; D002462:Cell Membrane / Q000648:ultrastructure*; D004548:Elasticity; D007091:Image Processing, Computer-Assisted; D007368:Interferometry; D008565:Membrane Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D008839:Microelectrodes; D018625:Microscopy, Atomic Force / Q000295:instrumentation* / Q000379:methods*; D008855:Microscopy, Electron, Scanning / Q000379:methods; D008954:Models, Biological; D020836:Protein Structure, Quaternary; D013057:Spectrum Analysis / Q000379:methods
D008565:Membrane Proteins