Microscopy interaction

Blends of polyethylene terephthalate and linear low-density polyethylene were compatibilised using diethylmaleate grafted polyethylene, and characterised using Fourier transform infra-red spectroscopy, thermogravimetric analysis and scanning electron microscopy. Interactions between the components in the blends were observed, which affected the glycol sequences of the polyester and also improved the thermal oxidative stability of the blends. The introduction of the compatibiliser resulted in a particle size reduction of the dispersed phase and better adhesion between the phase and the matrix. 15 refs. 

Two nucleation processes important to many people (including some surface scientists ) occur in the formation of gallstones in human bile and kidney stones in urine. Cholesterol crystallization in bile causes the formation of gallstones. Cryotransmission microscopy (Chapter VIII) studies of human bile reveal vesicles, micelles, and potential early crystallites indicating that the cholesterol crystallization in bile is not cooperative and the true nucleation time may be much shorter than that found by standard clinical analysis by light microscopy [75]. Kidney stones often form from crystals of calcium oxalates in urine. Inhibitors can prevent nucleation and influence the solid phase and intercrystallite interactions [76, 77]. Citrate, for example, is an important physiological inhibitor to the formation of calcium renal stones. Electrokinetic studies (see Section V-6) have shown the effect of various inhibitors on the surface potential and colloidal stability of micrometer-sized dispersions of calcium oxalate crystals formed in synthetic urine [78, 79]. 

Protein adsorption has been studied with a variety of techniques such as ellipsome-try [107,108], ESCA [109], surface forces measurements [102], total internal reflection fluorescence (TIRE) [103,110], electron microscopy [111], and electrokinetic measurement of latex particles [112,113] and capillaries [114], The TIRE technique has recently been adapted to observe surface diffusion [106] and orientation [IIS] in adsorbed layers. These experiments point toward the significant influence of the protein-surface interaction on the adsorption characteristics [105,108,110]. A very important interaction is due to the hydrophobic interaction between parts of the protein and polymeric surfaces [18], although often electrostatic interactions are also influential [ 116]. Protein desorption can be affected by altering the pH [117] or by the introduction of a complexing agent [118]. 

These authors doubt that such interactions can be estimated other than empirically without fairly accurate knowledge of the structure in the interfacial region. Sophisticated scattering, surface force, and force microscopy measurements are contributing to this knowledge however, a complete understanding is still a long way off. Even submonolayer amounts of adsorbed species can affect adhesion as found in metals and oxides [74]. 

The interest in vesicles as models for cell biomembranes has led to much work on the interactions within and between lipid layers. The primary contributions to vesicle stability and curvature include those familiar to us already, the electrostatic interactions between charged head groups (Chapter V) and the van der Waals interaction between layers (Chapter VI). An additional force due to thermal fluctuations in membranes produces a steric repulsion between membranes known as the Helfrich or undulation interaction. This force has been quantified by Sackmann and co-workers using reflection interference contrast microscopy to monitor vesicles weakly adhering to a solid substrate [78]. Membrane fluctuation forces may influence the interactions between proteins embedded in them [79]. Finally, in balance with these forces, bending elasticity helps determine shape transitions [80], interactions between inclusions [81], aggregation of membrane junctions [82], and unbinding of pinched membranes [83]. Specific interactions between membrane embedded receptors add an additional complication to biomembrane behavior. These have been stud-... 

With the exception of the scanning probe microscopies, most surface analysis teclmiques involve scattering of one type or another, as illustrated in figure A1.7.11. A particle is incident onto a surface, and its interaction with the surface either causes a change to the particles energy and/or trajectory, or the interaction induces the emission of a secondary particle(s). The particles that interact with the surface can be electrons, ions, photons or even heat. An analysis of the mass, energy and/or trajectory of the emitted particles, or the dependence of the emitted particle yield on a property of the incident particles, is used to infer infomiation about the surface. Although these probes are indirect, they do provide reliable infomiation about the surface composition and structure. 

The history of EM (for an overview see table Bl.17,1) can be interpreted as the development of two concepts the electron beam either illuminates a large area of tire sample ( flood-beam illumination , as in the typical transmission electron microscope (TEM) imaging using a spread-out beam) or just one point, i.e. focused to the smallest spot possible, which is then scaimed across the sample (scaiming transmission electron microscopy (STEM) or scaiming electron microscopy (SEM)). In both situations the electron beam is considered as a matter wave interacting with the sample and microscopy simply studies the interaction of the scattered electrons. 

While the spatial resolution in classical microscopy is limited to approximately X/2, where X is the optical wavelength (tlie so-called Abbe Limit [194], -0.2 pm with visible light), SNOM breaks through this barrier by monitoring the evanescent waves (of high spatial frequency) which arise following interaction with an... 

Durig U, Zuger O and Staider A 1992 interaction force detection in scanning probe microscopy methods and appiications J. Appl. Phys. 72 1778... 

Perez R, Payne M C, Stich i and Terakura K 1997 Roie of covaient tip-surface interactions in noncontact atomic force microscopy on reactive surfaces Phys. Rev. Lett. 78 678... 

Lee G U, Kidwell D A and Colton R J 1994 Sensing discrete streptavidin-biotin interactions with atomic force microscopy Langmuir 10 354... 

Detailed x-ray diffraction studies on polar liquid crystals have demonstrated tire existence of multiple smectic A and smectic C phases [M, 15 and 16]. The first evidence for a smectic A-smectic A phase transition was provided by tire optical microscopy observations of Sigaud etal [17] on binary mixtures of two smectogens. Different stmctures exist due to tire competing effects of dipolar interactions (which can lead to alternating head-tail or interdigitated stmctures) and steric effects (which lead to a layer period equal to tire molecular lengtli). These... 

Adechanical stahility. ChemisoriDtion to tire surface, intennolecular interactions and crosslinking between adjacent compounds—if possible—all contribute to tire resulting stability of tire monolayer film. Lateral force microscopy investigations revealed tliat tire mechanical stability towards lateral forces on tire nanometre scale is likely to be detennined by tire defect density and tire domain size on a nano- to micrometre scale [163, 1731. 

Particles can be manipulated in suspension using strongly focused laser beams ( optical tweezers ) [25] or magnetic fields [26] and by collecting statistics on tire particle movements using video microscopy, infonnation on the particle interactions can be obtained. 

Surfaces can be characterized using scaiming probe microscopies (see section B1.19). In addition, by attaching a colloidal particle to tire tip of an atomic force microscope, colloidal interactions can be probed as well [27]. Interactions between surfaces can be studied using tire surface force apparatus (see section B1.20). This also helps one to understand tire interactions between colloidal particles. 

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. 

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