Size methods ultracentrifuge

The size-selective precipitation (SPP) was predominantly developed by Pileni [50c]. One example (SPP) is monodisperse silver particles (2.3 nm, 0= 15%), which are precipitated from a polydisperse silver colloid solution in hexane by the addition of pyridine in three iterative steps. Recently, Schmid [52a] has reported the two-dimensional crystallization of truly monodisperse AU55 clusters. Chromatographic separation methods have thus far proven unsuccessful because the colloid decomposed after the colloidal protecting shell had been stripped off [42a]. The size-selective ultracentrifuge separation of Pt colloids has been developed by Colfen [52b]. Although this elegant separation method gives truly monodisperse metal... 

Note that this method of standardizing D values makes no allowance for the possibility that a molecule may change size, shape, or solvation with changes in temperature. In the next section we shall survey the behavior of polymeric materials in an ultracentrifuge. We shall see that diffusion coefficients can be... 

Separation methods based on size include size exclusion chromatography, ultra-filtration, and ultracentrifugation (see Chapter Appendix). The ionic properties of peptides and proteins are determined principally by their complement of amino acid side chains. Furthermore, the ionization of these groups is pH-dependent. 

There are various methods for the determination of the size distribution of organic pigment particles, the most common are sedimentation techniques in ultracentrifuges and specialized disk centrifuges as well as electron microscopy. These methods require considerable experimental skill, since the results depend largely on sample preparation and especially on the quality of the dispersion. 

To determine the shape of ribosomal proteins in solution, ultracentrifugation, digital densimetry, viscosity, gel filtration, quasi-elastic light scattering, and small-angle X-ray or neutron scattering have all been used. With each technique it is possible to obtain a physical characteristic of the protein. Combining these techniques should allow the size and shape of the protein to be characterized quite well. However, the values determined in various laboratories for the same ribosomal proteins differ considerably. To help understand some of the reasons we will initially discuss each method briefly as it relates to proteins and then review the size and shape of the ribosomal proteins that have been so characterized. 

A basic limitation of all these methods is the narrow range of particle sizes that can be investigated by sedimentation under gravity. Therefore, we turn next to a consideration of centrifugation, particularly the ultracentrifuge, as a means of extending the applicability of sedimentation measurements. 

The syntheses of heterostranded coiled coils are presented (Section 13.2.2.4), as are templates and conformationally defined peptide libraries (Sections 13.2.4 and 13.2.4.1). Finally, Section 13.1 concludes with a presentation of the methods for characterization of the coiled coils including circular dichroism, microcalorimetry, size-exclusion chromatography, and analytical ultracentrifugation (Section 13.2.5). 

Many of the methods used to extract information related to the structure of macromolecules come from studying the behavior of isolated macromolecules in solution. These techniques are based primarily on the flow behavior in a velocity gradient, the rate of Brownian motion of a particle, or osmotic effects associated with the size of individual molecules. The techniques that have been employed to study size and shape of macromolecules most extensively include viscometry, light scattering, analytical ultracentrifugation, and electron microscopy. 

Another method for determining homogeneity and molecular size of antibodies is density gradient ultracentrifugation [33], A sample of anti-... 

---