Keine ausfuhrliche Beschreibung fur "e;Extraktive Aufarbeitung bestrahlter Kernbrennstoffe"e; verfugbar.

Metal clusters are on the brink between molecules and nanoparticles in size. With molecular, nano-scale, metallic as well as non-metallic aspects, metal clusters are a growing, interdisciplinary field with numerous potential applications in chemistry, catalysis, materials and nanotechnology. This third volume in the series of hot topics from inorganic chemistry covers all recent developments in the field of metal clusters, with some 20 contributions providing an in-depth view. The result is a unique perspective, illustrating all facets of this interdisciplinary area: * Inter-electron Repulsion and Irregularities in the Chemistry of Transition Series * Stereochemical Activity of Lone Pairs in Heavier Main Group Element Compounds * How Close to Close Packing? * Forty-Five Years of Praseodymium Diiodide * Centered Zirconium Clusters * Titanium Niobium Oxychlorides * Trinuclear Molybdenum and Tungsten Cluster Chalcogenides * Current State of (B,C,N)-Compounds of Calcium and Lanthanum * Ternary Phases of Lithium with Main-Group and Late-Transition Metals * Polar Intermetallics and Zintl Phases along the Zintl Border * Rare Earth Zintl Phases * Structure-Property Relationships in Intermetallics * Ternary and Quaternary Niobium Arsenide Zintl Phases * The Building Block Approach to Understanding Main-Group-Metal Complex Structures * Cation-Deficient Quaternary Thiospinels * A New Class of Hybrid Materials via Salt Inclusion Synthesis * Layered Perrhenate and Vanadate Hybrid Solids * Hydrogen Bonding in Metal Halides * Syntheses and Catalytic Properties of Titanium Nitride Nanoparticles * Solventless Thermolysis * New Potential Scintillation Materials in Borophosphate Systems. With its didactical emphasis, this volume addresses a wide readership, such that both students and specialists will profit from the expert contributions.

Infrared spectroscopy is a new and innovative technology to study protein folding/misfolding events in the broad arsenal of techniques conventionally used in this field. The progress in understanding protein folding and misfolding is primarily due to the development of biophysical methods which permit to probe conformational changes with high kinetic and structural resolution. The most commonly used approaches rely on rapid mixing methods to initiate the folding event via a sudden change in solvent conditions. Traditionally, techniques such as fluorescence, circular dichroism or visible absorption are applied to probe the process. In contrast to these techniques, infrared spectroscopy came into play only very recently, and the progress made in this field up to date which now permits to probe folding events over the time scale from picoseconds to minutes has not yet been discussed in a book. The aim of this book is to provide an overview of the developments as seen by some of the main contributors to the field. The chapters are not intended to give exhaustive reviews of the literature but, instead to illustrate examples demonstrating the sort of information, which infrared techniques can provide and how this information can be extracted from the experimental data. By discussing the strengths and limitations of the infrared approaches for the investigation of folding and misfolding mechanisms this book helps the reader to evaluate whether a particular system is appropriate for studies by infrared spectroscopy and which specific advantages the techniques offer to solve specific problems.

Infrared spectroscopy is a new and innovative technology to study protein folding/misfolding events in the broad arsenal of techniques conventionally used in this field. The progress in understanding protein folding and misfolding is primarily due to the development of biophysical methods which permit to probe conformational changes with high kinetic and structural resolution. The most commonly used approaches rely on rapid mixing methods to initiate the folding event via a sudden change in solvent conditions. Traditionally, techniques such as fluorescence, circular dichroism or visible absorption are applied to probe the process. In contrast to these techniques, infrared spectroscopy came into play only very recently, and the progress made in this field up to date which now permits to probe folding events over the time scale from picoseconds to minutes has not yet been discussed in a book. The aim of this book is to provide an overview of the developments as seen by some of the main contributors to the field. The chapters are not intended to give exhaustive reviews of the literature but, instead to illustrate examples demonstrating the sort of information, which infrared techniques can provide and how this information can be extracted from the experimental data. By discussing the strengths and limitations of the infrared approaches for the investigation of folding and misfolding mechanisms this book helps the reader to evaluate whether a particular system is appropriate for studies by infrared spectroscopy and which specific advantages the techniques offer to solve specific problems.

Infrared spectroscopy is a new and innovative technology to study protein folding/misfolding events in the broad arsenal of techniques conventionally used in this field. The progress in understanding protein folding and misfolding is primarily due to the development of biophysical methods which permit to probe conformational changes with high kinetic and structural resolution. The most commonly used approaches rely on rapid mixing methods to initiate the folding event via a sudden change in solvent conditions. Traditionally, techniques such as fluorescence, circular dichroism or visible absorption are applied to probe the process. In contrast to these techniques, infrared spectroscopy came into play only very recently, and the progress made in this field up to date which now permits to probe folding events over the time scale from picoseconds to minutes has not yet been discussed in a book. The aim of this book is to provide an overview of the developments as seen by some of the main contributors to the field. The chapters are not intended to give exhaustive reviews of the literature but, instead to illustrate examples demonstrating the sort of information, which infrared techniques can provide and how this information can be extracted from the experimental data. By discussing the strengths and limitations of the infrared approaches for the investigation of folding and misfolding mechanisms this book helps the reader to evaluate whether a particular system is appropriate for studies by infrared spectroscopy and which specific advantages the techniques offer to solve specific problems.

Keine ausfuhrliche Beschreibung fur "e;Extraktive Aufarbeitung bestrahlter Kernbrennstoffe"e; verfugbar.

Metal clusters are on the brink between molecules and nanoparticles in size. With molecular, nano-scale, metallic as well as non-metallic aspects, metal clusters are a growing, interdisciplinary field with numerous potential applications in chemistry, catalysis, materials and nanotechnology. This third volume in the series of hot topics from inorganic chemistry covers all recent developments in the field of metal clusters, with some 20 contributions providing an in-depth view. The result is a unique perspective, illustrating all facets of this interdisciplinary area: * Inter-electron Repulsion and Irregularities in the Chemistry of Transition Series * Stereochemical Activity of Lone Pairs in Heavier Main Group Element Compounds * How Close to Close Packing? * Forty-Five Years of Praseodymium Diiodide * Centered Zirconium Clusters * Titanium Niobium Oxychlorides * Trinuclear Molybdenum and Tungsten Cluster Chalcogenides * Current State of (B,C,N)-Compounds of Calcium and Lanthanum * Ternary Phases of Lithium with Main-Group and Late-Transition Metals * Polar Intermetallics and Zintl Phases along the Zintl Border * Rare Earth Zintl Phases * Structure-Property Relationships in Intermetallics * Ternary and Quaternary Niobium Arsenide Zintl Phases * The Building Block Approach to Understanding Main-Group-Metal Complex Structures * Cation-Deficient Quaternary Thiospinels * A New Class of Hybrid Materials via Salt Inclusion Synthesis * Layered Perrhenate and Vanadate Hybrid Solids * Hydrogen Bonding in Metal Halides * Syntheses and Catalytic Properties of Titanium Nitride Nanoparticles * Solventless Thermolysis * New Potential Scintillation Materials in Borophosphate Systems. With its didactical emphasis, this volume addresses a wide readership, such that both students and specialists will profit from the expert contributions.

Infrared spectroscopy is a new and innovative technology to study protein folding/misfolding events in the broad arsenal of techniques conventionally used in this field. The progress in understanding protein folding and misfolding is primarily due to the development of biophysical methods which permit to probe conformational changes with high kinetic and structural resolution. The most commonly used approaches rely on rapid mixing methods to initiate the folding event via a sudden change in solvent conditions. Traditionally, techniques such as fluorescence, circular dichroism or visible absorption are applied to probe the process. In contrast to these techniques, infrared spectroscopy came into play only very recently, and the progress made in this field up to date which now permits to probe folding events over the time scale from picoseconds to minutes has not yet been discussed in a book. The aim of this book is to provide an overview of the developments as seen by some of the main contributors to the field. The chapters are not intended to give exhaustive reviews of the literature but, instead to illustrate examples demonstrating the sort of information, which infrared techniques can provide and how this information can be extracted from the experimental data. By discussing the strengths and limitations of the infrared approaches for the investigation of folding and misfolding mechanisms this book helps the reader to evaluate whether a particular system is appropriate for studies by infrared spectroscopy and which specific advantages the techniques offer to solve specific problems.

Infrared spectroscopy is a new and innovative technology to study protein folding/misfolding events in the broad arsenal of techniques conventionally used in this field. The progress in understanding protein folding and misfolding is primarily due to the development of biophysical methods which permit to probe conformational changes with high kinetic and structural resolution. The most commonly used approaches rely on rapid mixing methods to initiate the folding event via a sudden change in solvent conditions. Traditionally, techniques such as fluorescence, circular dichroism or visible absorption are applied to probe the process. In contrast to these techniques, infrared spectroscopy came into play only very recently, and the progress made in this field up to date which now permits to probe folding events over the time scale from picoseconds to minutes has not yet been discussed in a book. The aim of this book is to provide an overview of the developments as seen by some of the main contributors to the field. The chapters are not intended to give exhaustive reviews of the literature but, instead to illustrate examples demonstrating the sort of information, which infrared techniques can provide and how this information can be extracted from the experimental data. By discussing the strengths and limitations of the infrared approaches for the investigation of folding and misfolding mechanisms this book helps the reader to evaluate whether a particular system is appropriate for studies by infrared spectroscopy and which specific advantages the techniques offer to solve specific problems.

Infrared spectroscopy is a new and innovative technology to study protein folding/misfolding events in the broad arsenal of techniques conventionally used in this field. The progress in understanding protein folding and misfolding is primarily due to the development of biophysical methods which permit to probe conformational changes with high kinetic and structural resolution. The most commonly used approaches rely on rapid mixing methods to initiate the folding event via a sudden change in solvent conditions. Traditionally, techniques such as fluorescence, circular dichroism or visible absorption are applied to probe the process. In contrast to these techniques, infrared spectroscopy came into play only very recently, and the progress made in this field up to date which now permits to probe folding events over the time scale from picoseconds to minutes has not yet been discussed in a book. The aim of this book is to provide an overview of the developments as seen by some of the main contributors to the field. The chapters are not intended to give exhaustive reviews of the literature but, instead to illustrate examples demonstrating the sort of information, which infrared techniques can provide and how this information can be extracted from the experimental data. By discussing the strengths and limitations of the infrared approaches for the investigation of folding and misfolding mechanisms this book helps the reader to evaluate whether a particular system is appropriate for studies by infrared spectroscopy and which specific advantages the techniques offer to solve specific problems.