Dynamic atomic force microscopy

Garcia R, Perez R (2002) Dynamic atomic force microscopy methods. Surf Sci Rep 47 197-301... 

Deleu, M., Nott, K., Brasseur, R., Jacques, R, Thonart, R, and Dufrene, Y. F. 2001. Imaging mixed lipid monolayers by dynamic atomic force microscopy, Biochim Biophys Acta 1513,55-62. 

C. Carrasco, P. Ares, P. J. de Pablo, and J. GOmez-Herrero, Cutting down the forest of peaks in acoustic dynamic atomic force microscopy in liquid. Rev. Sci. Instrum. 79,126106 (2008]. 

S. Kawai, D. Kobayashi, S. Kitamura, S. Meguro, and H. Kawakatsu, An ultrahigh vacuum dynamic force microscope for high resonance frequency cantilevers. Rev. Sci. Instrum. 76,083703 (20053-S. Nishida, D. Kobayashi, T. Sakurada, T. Nakazawa, Y. Hoshi, and H. Kawakatsu, Photothermal excitation and laser doppler veloclmetry of higher cantilever vibration modes for dynamic atomic force microscopy in liquid. Rev. Sci. Instrum. 79,123703 (2008J. 

Garcia R, Gomez CJ, Martinez NF, Patil S, Dietz C, Magerle R. Identification of nanoscale dissipation processes by dynamic atomic force microscopy. Phys Rev Lett 2006 97 016103 (4pp). 

Flenderson E, Flaydon P G and Sakaguchi D S 1992 Actin filament dynamics in living glial cells imaged by atomic force microscopy Science 257 1944... 

Abstract. Molecular dynamics (MD) simulations of proteins provide descriptions of atomic motions, which allow to relate observable properties of proteins to microscopic processes. Unfortunately, such MD simulations require an enormous amount of computer time and, therefore, are limited to time scales of nanoseconds. We describe first a fast multiple time step structure adapted multipole method (FA-MUSAMM) to speed up the evaluation of the computationally most demanding Coulomb interactions in solvated protein models, secondly an application of this method aiming at a microscopic understanding of single molecule atomic force microscopy experiments, and, thirdly, a new method to predict slow conformational motions at microsecond time scales. 

Anezykowski, B., Gotsmann, B., Fuchs, H., Cleveland, J.P. and Elings, V.B., How to measure energy dissipation in dynamic mode atomic force microscopy. AppL Surf. Sci., 140, 376-382 (1999). 

Pandey et al. have used ultrasonic velocity measurement to study compatibility of EPDM and acrylonitrile-butadiene rubber (NBR) blends at various blend ratios and in the presence of compa-tibilizers, namely chloro-sulfonated polyethylene (CSM) and chlorinated polyethylene (CM) [22]. They used an ultrasonic interferometer to measure sound velocity in solutions of the mbbers and then-blends. A plot of ultrasonic velocity versus composition of the blends is given in Eigure 11.1. Whereas the solution of the neat blends exhibits a wavy curve (with rise and fall), the curves for blends with compatibihzers (CSM and CM) are hnear. They resemble the curves for free energy change versus composition, where sinusoidal curves in the middle represent immiscibility and upper and lower curves stand for miscibihty. Similar curves are obtained for solutions containing 2 and 5 wt% of the blends. These results were confirmed by measurements with atomic force microscopy (AEM) and dynamic mechanical analysis as shown in Eigures 11.2 and 11.3. Substantial earher work on binary and ternary blends, particularly using EPDM and nitrile mbber, has been reported. 

Hizume K, Yoshimura SH, Maruyama H, Kim J, Wada H, Takeyasu K (2002) Chromatin reconstitution development of a salt-dialysis method monitored by nano-technology. Arch Histol Cytol 65 405 13 Hizume K, Yoshimura SH, Takeyasu K (2004) Atomic force microscopy demonstrates a critical role of DNA superhelicity in nucleosome dynamics. Cell Biochem Biophys 40 249—262 Hizume K, Yoshimura SH, Takeyasu K (2005) Linker histone HI per se can induce three-dimensional folding of chromatin fiber. Biochemistry 44 12978-12989 Hofmann WA, de Lanerolle P (2006) Nuclear actin to polymerize or not to polymerize. J Cell Biol 172 495-496... 

Pursch, M., Vanderhart, D.L., Sander, L.C., Gu, X., Nguyen, T., and Wise, S.A., C30 self-assembled monolayers on sihca, titania and zirconia HPLC performance, atomic force microscopy and NMR studies of molecular dynamics and uniformity of coverage, J. Am. Chem. Soc., 6997, 2000. 

To characterize dendrimers, analytical methods used in synthetic organic chemistry as well as in macromolecular chemistry can be applied. Mass spectrometry and NMR spectroscopy are especially useful tools to estimate purity and structural perfection. To get an idea of the size of dendrimers, direct visualization methods such as atomic force microscopy (AFM) and transmission electron microscopy (TEM), or indirect methods such as size exclusion chromatography (SEC) or viscosimetry, are valuable. Computer aided simulation also became a very useful tool not only for the simulation of the geometry of a distinct molecule, but also for the estimation of the dynamics in a dendritic system, especially concerning mobility, shape-persistence, and end-group disposition. 

Higgins S.R., Boram L.H., Eggleston C.M., Coles B.A., Compton R.G., and Knauss K.G. (2002a) Dissolution kinetics, step and surface morphology of magnesite (104) surfaces in acidic aqueous solution at 60°C by atomic force microscopy under defined hydro-dynamic conditions. /. Phys. Chem. B 106, 6696-6705. 

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