Application of thermal analysis to carbon black-elastomer systems

In this study a relationship between the surface and textural properties of carbon blacks and the gasification process induced thermally in air is noted. A temperature jump method was used to follow the gasification in air and to establish the relevant Arrhenius parameters. This can be associated with the activity of ‘basal’ plane carbon atoms as well as ‘edge’ carbon atoms at the surface. This is based on a model of carbon black structure consisting of the irregular packing of small graphite carbon structures. The carbon black surface was measured using a single measurement of adsorption based essentially on the BET volumetric method. The carbon black surface had a rate of oxidation per unit are which clearly indicated that the lower area carbon blacks had a predominately active area of ‘edge’ atoms at the surface while the surface of the higher area carbon blacks had a predominate amount of ‘basal’ plane graphite carbon atoms.     

Fractional Brownian dynamics in proteins

Correlation functions describing relaxation processes in proteins and other complex molecular systems are known to exhibit a nonexponential decay. The simulation study presented here shows that fractional Brownian dynamics is a good model for the internal dynamics of a lysozyme molecule in solution. We show that both the dynamic structure factor and the associated memory function fit well the corresponding analytical functions calculated from the model. The numerical analysis is based on autoregressive modeling of time series.     

An effective method for the discrimination of motional anisotropy and chemical exchange

Analysis of the ratio of transverse and longitudinal relaxation rates (R2/R1) is an approach commonly used for estimation of overall correlation time and identification of chemical exchange in biological macromolecules. However, this analysis fails to distinguish between chemical exchange and motional anisotropy. We describe a simple method for identifying chemical exchange and motional anisotropy using the product, R1R2. In the slow tumbling regime, the R1R2 product results in a constant value that is independent of overall correlation time and motional anisotropy. This analysis provides a simple method for rapidly estimating and dissociating the effects of motional anisotropy and chemical exchange in NMR heteronuclear spin relaxation data. We demonstrate the utility of the method with 15N relaxation data collected on the proteins E. coli ribonuclease H and the trimeric E. coli membrane associated lipoprotein lpp.