New PDF release: Atomic Force Microscopy in Cell Biology, Volume 68

By Bhanu P. Jena

ISBN-10: 0125441711

ISBN-13: 9780125441711

This can be the 1st booklet to hide the background, constitution, and alertness of atomic strength microscopy in cellphone biology. provided within the transparent, well-illustrated form of the Methods in mobile Biology sequence, it introduces the AFM to its readers and allows them to faucet the ability and scope of this expertise to additional their very own examine. a pragmatic laboratory consultant to be used of the atomic strength and photonic strength microscopes, it offers up-to-date expertise and techniques in strength spectroscopy. it's also a finished and easy-to-follow useful laboratory consultant for using the AFM and PFM in organic learn.

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Additional info for Atomic Force Microscopy in Cell Biology, Volume 68

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5 μm in diameter, at the plasma membrane following stimulation (Spudich and Braunstein, 1995). The authors suggest that these structures may be involved in membrane retrieval following intense stimulation of these cells. The AFM has thus enabled the identification of pits at the cell surface and the study of their dynamics over time following stimulation of secretion in live rat basophilic leukemia cells. , 2000). This study showed the capability of the AFM to measure adhesion of live cells on different substrates and provided new information on medical implant research.

P. (1991). In “Scanned Probe Microscopies: STM and Beyond” (H. ), p. 241. AIP Conference Proceedings. H¨orber, J. K. , Schuler, F. , Schr¨oter, K. , and Ruppersberg, J. P. (1991). J. Vac. Sci. Technol. B9, 1214. , and Hudspeth, A. J. (1988). Neuron 1, 189. Hudspeth, A. J. (1983). Annu. Rev. Neurosci. 6, 187. , Florin, Ernst-Ludwig, and H¨orber, J. K. H. (2001). ). Humana Press Inc. Totowa, NJ. , and Simons, K. (1998). J. Cell Biol. 140, 1357. Kellermayer, M. S. , Smith, S. , Granzier, H. , and Bustamante, C.

In the sawtooth-like pattern of the force– extension curves, each peak represents the breaking of the major stabilizing connection. After each peak, the force drops back as the additional length of the protein chain becomes available. The maximal extension in these experiments is variable as the polymer either is not always picked up at the end or has attached at more than one site to the surface. 6 nm for the spectrin chain. Two consecutive force peaks are spaced by a distance that represents the gain in length produced by a single unfolding event.

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Atomic Force Microscopy in Cell Biology, Volume 68 by Bhanu P. Jena

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