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1 Introduction.- 2 Neutron Scattering and Neutron Spin Echo.- 3 Large Scale Dynamics of Homopolymers.-
Dynamics of Soft Matter: Neutron Applications provides an overview of neutron scattering techniques that measure temporal and spatial correlations simultaneously, at the microscopic and/or mesoscopic scale. These techniques offer answers to new questions arising at the interface of physics, chemistry, and biology. Knowledge of the dynamics at these levels is crucial to understanding the soft matter field, which includes colloids, polymers, membranes, biological macromolecules, foams, emulsions towards biological & biomimetic systems, and phenomena involving wetting, friction, adhesion, or microfluidics. Emphasizing the complementarities of scattering techniques with other spectroscopic ones, this volume also highlights the potential gain in combining techniques such as rheology, NMR, light scattering, dielectric spectroscopy, as well as synchrotron radiation experiments. Key areas covered include polymer science, biological materials, complex fluids and surface science.
The dielectric properties especially of glassy materials are nowadays explored at widely varying temperatures and pressures without any gap in the spectral range from μHz up to the Infrared, thus covering typically 20 decades or more. This extraordinary span enables to trace the scaling and the mutual interactions of relaxation processes in detail, e.g. the dynamic glass transition and secondary relaxations, but as well far infrared vibrations, like the Boson peak. Additionally the evolution of intra-molecular interactions in the course of the dynamic glass transition is also well explored by (Fourier Transform) Infrared Spectroscopy. This volume within 'Advances in Dielectrics' summarizes this knowledge and discusses it with respect to the existing and often competing theoretical concepts.
Disordered proteins are relatively recent newcomers in protein science. They were first described in detail by Wright and Dyson, in their J. Mol. Biol. paper in 1999. First, it was generally thought for more than a decade that disordered proteins or disordered parts of proteins have different amino acid compositions than folded proteins, and various prediction methods were developed based on this principle. These methods were suitable for distinguishing between the disordered (unstructured) and structured proteins known at that time. In addition, they could predict the site where a folded protein binds to the disordered part of a protein, shaping the latter into a well-defined 3D structure. ...
This first book on this important and emerging topic presents an overview of the very latest results obtained in single-chain polymer nanoparticles obtained by folding synthetic single polymer chains, painting a complete picture from synthesis via characterization to everyday applications. The initial chapters describe the synthetics methods as well as the molecular simulation of these nanoparticles, while subsequent chapters discuss the analytical techniques that are applied to characterize them, including size and structural characterization as well as scattering techniques. The final chapters are then devoted to the practical applications in nanomedicine, sensing, catalysis and several other uses, concluding with a look at the future for such nanoparticles. Essential reading for polymer and materials scientists, materials engineers, biochemists as well as environmental chemists.
This book provides an introduction to the basic principles of neutron scattering and its application to current problems in condensed matter science and technology. Experiments on novel materials are particularly emphasized.
Aimed at students, lecturers, researchers, and policy makers, this work describes current developments and points the way forward for new developments regarding materials in our society and how they relate to sustainability.