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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 α and polyproline helices and their complexes, the α-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.
Volume 323 of Methods in Enzymology is dedicated to the energetics of biological macromolecules. Understanding the molecular mechanisms underlying a biological process requires detailed knowledge of the structural relationships within the system and an equally detailed understanding of the energetic driving forces that control the structural interactions. This volume presents modern thermodynamic techniques currently being utilized to study the energetic driving forces in biological systems. It will be a useful reference source and textbook for scientists and students whose goal is to understand the energetic relationships between macromoleculer structures and biological functions. This volume supplements Volumes 259 and Volume 295 of Methods in Enzymology.Key Features* Probing Stability of Helical Transmembrane Proteins* Energetics of Vinca Alkaloid Interactions with Tubulin* Deriving Complex Ligand Binding Formulas* Mathematical Modeling of Cooperative Interactions in Hemoglobin* Analysis of Interactions of Regulatory Protein TyrR with DNA* Parsing Free Energy of Drug-DNA Interactions* Use of Fluorescence as Thermodynamics Tool
6th European Conference on the Spectroscopy of Biological Molecules, 3--8 September 1995, Villeneuve d'Ascq, France
This volume provides methods on microcalorimetry approaches to investigate complex biological molecular systems. Chapters guide readers through Differential Scanning Calorimetry (DSC), Isothermal Titration Calorimetry (ITC), and advanced data processing. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and practical, Microcalorimetry of Biological Molecules: Methods and Protocols aims to ensure successful results in the further study of this vital field.
Calorimetry, as a technique for thermal analysis, has a wide range of applications which are not only limited to studying the thermal characterisation (e.g. melting temperature, denaturation temperature and enthalpy change) of small and large drug molecules, but are also extended to characterisation of fuel, metals and oils. Differential Scanning Calorimetry is used to study the thermal behaviours of drug molecules and excipients by measuring the differential heat flow needed to maintain the temperature difference between the sample and reference cells equal to zero upon heating at a controlled programmed rate. Microcalorimetry is used to study the thermal transition and folding of biological macromolecules in dilute solutions. Microcalorimetry is applied in formulation and stabilisation of therapeutic proteins. This book presents research from all over the world on the applications of calorimetry on both solid and liquid states of materials.
Nuclear Magnetic Resonance (NMR) spectroscopy is the most powerful technique for characterization of biomolecular structures at atomic resolution in the solution state. This timely book, entitled "Biomolecular NMR Spectroscopy," focuses on the latest state-of-the-art NMR techniques for characterization of biological macromolecules in the solid and solution state. The editors, Dr. Andrew Dingley (University of Auckland, New Zealand) and Dr. Steven Pascal (Massey University, New Zealand) have organized the book into four sections, covering the following topics: sample preparation, structure and dynamics of proteins, structure and dynamics of nucleic acids and protein-nucleic acid complexes, and rapid and hybrid techniques--
Our knowledge of biological macromolecules and their interactions is based on the application of physical methods, ranging from classical thermodynamics to recently developed techniques for the detection and manipulation of single molecules. These methods, which include mass spectrometry, hydrodynamics, microscopy, diffraction and crystallography, electron microscopy, molecular dynamics simulations, and nuclear magnetic resonance, are complementary; each has its specific advantages and limitations. Organised by method, this textbook provides descriptions and examples of applications for the key physical methods in modern biology. It is an invaluable resource for undergraduate and graduate students of molecular biophysics in science and medical schools, as well as research scientists looking for an introduction to techniques beyond their specialty. As appropriate for this interdisciplinary field, the book includes short asides to explain physics aspects to biologists and biology aspects to physicists.
Current techniques for studying biological macromolecules and their interactions are based on the application of physical methods, ranging from classical thermodynamics to more recently developed techniques for the detection and manipulation of single molecules. Reflecting the advances made in biophysics research over the past decade, and now including a new section on medical imaging, this new edition describes the physical methods used in modern biology. All key techniques are covered, including mass spectrometry, hydrodynamics, microscopy and imaging, diffraction and spectroscopy, electron microscopy, molecular dynamics simulations and nuclear magnetic resonance. Each method is explained in detail using examples of real-world applications. Short asides are provided throughout to ensure that explanations are accessible to life scientists, physicists and those with medical backgrounds. The book remains an unparalleled and comprehensive resource for graduate students of biophysics and medical physics in science and medical schools, as well as for research scientists looking for an introduction to techniques from across this interdisciplinary field.
The critically acclaimed laboratory standard, Methods in Enzymology, is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. The series contains much material still relevant today - truly an essential publication for researchers in all fields of life sciences.
Calorimetry, the latest volume in the Methods in Enzymology series continues the legacy of this premier serial with quality chapters authored by leaders in the field. Calorimetry is a highly technical experiment and it is easy for new practioners to get fooled into interpreting artifacts as real experimental results. This volume will guide readers to get the most out of their precious biological samples and includes topics on specific protocols for the types of studies being conducted as well as tips to improve the data collection. Most importantly, the chapters will also help to identify pitfalls that need to be avoided to ensure that the highest quality results are obtained. - Contains timely contributions from recognized experts in this rapidly changing field - Provides specific protocols and tips to improve data collection and ensure the highest quality results are obtained - Covers research methods in calorimetry, and includes sections on topics such as differential scanning calorimetry of membrane and soluble proteins in detergents