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It was not until 1971 that the authority for defining scientific units, the General Conference of Weights and Measures got around to defining the unit that is the basis of chemistry (the mole, or the quantity of something). Yet for all this tardiness in putting the chemical sciences on a sound quantitative basis, chemistry is an old and venerable subject and one naturally asks the question, why? Well, the truth is that up until the mid-1920s, many physicists did not believe in the reality of molecules. Indeed, it was not until after the physics community had accepted Ernest Rutherford's 1913 solar-system-like model of the atom, and the quantum mechanical model of the coupling of electron spins in atoms that physicists started to take seriously the necessity of explaining the chemical changes that chemists had been observing, investigating and recording since the days of the alchemists.

Computational spectroscopy is a rapidly evolving field that is becoming a versatile and widespread tool for the assignment of experimental spectra and their interpretation as related to chemical physical effects. This book is devoted to the most significant methodological contributions in the field, and to the computation of IR, UV-VIS, NMR and EPR spectral parameters with reference to the underlying vibronic and environmental effects. Each section starts with a chapter written by an experimental spectroscopist dealing with present challenges in the different fields; comprehensive coverage of conventional and advanced spectroscopic techniques is provided by means of dedicated chapters written by experts. Computational chemists, analytical chemists and spectroscopists, physicists, materials scientists, and graduate students will benefit from this thorough resource.

Examining the physical basis of the structure of macromolecules—proteins, nucleic acids, and their complexes—using calorimetric techniques Many scientists working in biology are unfamiliar with the basics of thermodynamics and its role in determining molecular structures. Yet measuring the heat of structural change a molecule undergoes under various conditions yields information on the energies involved and, thus, on the physical bases of the considered structures. Microcalorimetry of Macromolecules offers protein scientists unique access to this important information. Divided into thirteen chapters, the book introduces readers to the basics of thermodynamics as it applies to calorimetry, the evolution of the calorimetric technique, as well as how calorimetric techniques are used in the thermodynamic studies of macromolecules, detailing instruments for measuring the heat effects of various processes. Also provided is general information on the structure of biological macromolecules, proteins, and nucleic acids, focusing on the key thermodynamic problems relating to their structure. The book covers: The use of supersensitive calorimetric instruments, including micro and nano-calorimeters for measuring the heat of isothermal reactions (Isothermal Titration Nano-Calorimeter), the heat capacities over a broad temperature range (Scanning Nano-Calorimeter), and pressure effects (Pressure Perturbation Nano-Calorimeter) Two of the simplest but key structural elements: the ? and polyproline helices and their complexes, the ?-helical coiled-coil, and the pyroline coiled-coils Complicated macromolecular formations, including small globular proteins, multidomain proteins and their complexes, and nucleic acids Numerous examples of measuring the ground state of protein energetics, as well as changes seen when proteins interact The book also reveals how intertwined structure and thermodynamics are in terms of a macromolecule's organization, mechanism of formation, the stabilization of its three-dimensional structure, and ultimately, its function. The first book to describe microcalorimetric technique in detail, enough for graduate students and research scientists to successfully plumb the structural mysteries of proteins and the double helix, Microcalorimetry of Macromolecules is an essential introduction to using a microcalorimeter in biological studies.

Explains and analyzes polymer physical chemistry research methods and experimental data Taking a fresh approach to polymer physical chemistry, Physical Properties of Macromolecules integrates the two foundations of physical polymer science, theory and practice. It provides the tools to understand polymer science concepts and research methods, while also instructing how to analyze experimental data. Drawing on the author's own extensive research in physical properties of polymers as well as more traditional topics, this text offers detailed analysis of numerous problems in polymer science, including laboratory data and research results. Topics include: Solid-state dynamics of polymeric materials Glass transitions in amorphous polymers Semicrystalline polymers and melting transitions Viscoelastic behavior Relaxation processes Macromolecule-metal complexes Mechanical properties of linear and crosslinked polymers Filled with detailed graphs to help explain important quantitative trends, Physical Properties of Macromolecules teaches by example, ensuring comprehension of the subject as well as the methodology to implement theory, problem-solving techniques, and research results in practical situations. This resource serves as the ideal companion for government laboratories, industrial research scientists, engineers, and professionals in polymer science fields who are interested in fully grasping all aspects of physical polymer science.

This book is a comprehensive study of the subject of ionic interactions in macromolecules. The first parts of the book review and analyze the conventional treatments of fixed charges (e.g. in polyelectrolytes and polyampholytes), including screening and condensation by mobile ions. The interaction of ions with less polar sites on the macromolecule (e.g. amide bonds), and the origin of the lyotropic effects (focusing on binding versus condensation) will also be extensively addressed. The book also explores complex micellar organizations involving charged macromolecules (e.g. DNA) and low-molecular-weight ampholytes and strong protein associations. The resulting structures are relevant to a variety of functional biological systems and synthetic analogs. The contribution of electrostatic and hydrophobic interaction to the stability of proteins and other supramolecular structures will also be analyzed. There are chapters on applications such as deionization and cosmetic formulation. This 21-chapter book is divided into three sections: Fundamentals Mixed Interactions Functions and Applications

Arising from a workshop, this book surveys the physics of ultracold atoms and molecules taking into consideration the latest research on ultracold phenomena, such as Bose Einstein condensation and quantum computing. Several reputed authors provide an introduction to the field, covering recent experimental results on atom and molecule cooling as well as the theoretical treatment.