Microcalorimetry of Macromolecules (PDF)
The Physical Basis of Biological Structures
(Sprache: Englisch)
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...
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...
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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 alpha and
polyproline helices and their complexes, the alpha-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.
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 alpha and
polyproline helices and their complexes, the alpha-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.
Inhaltsverzeichnis zu „Microcalorimetry of Macromolecules (PDF)“
1. Introduction 2. Methodology 2.1. Thermodynamic basis of calorimetry 2.2. Equilibrium analysis 2.3. Aqueous solutions 2.4. Transfer of solutes into the aqueous phase 3. Calorimetry 3.1. Isothermal reaction microcalorimetry 3.2. Heat capacity calorimetry 3.3. Pressure perturbation calorimetry 4. Macromolecules 4.1. Evolution of the concept 4.2. Proteins 4.3. Hierarchy in protein structure 4.4. Nucleic Acids 5. The a-helix and a-helical coiled coil 5.1. The a-helix 5.2. The a-helical coiled-coils 5.3. The a-helical coiled-coil proteins 6. Polyproline-II coiled-coils 6.1. Collagens 6.2. Calorimetric studies of collagens 6.3. Thermodynamics of collagen 7. Globular proteins 7.1. Denaturation of globular proteins 7.2. Heat denaturation of proteins 7.3. Cold denaturation 7.4. The pH induced protein denaturation 7.5. Denaturant induced protein unfolding 7.6. Unfolded state of protein 8. Energetic basis of protein structure 8.1. Hydration effects 8.2. Protein in vacuum 8.3. Back into the water 9. Protein folding 9.1. Macro and micro stabilities of protein structure 9.2. Protein folding technology 9.3. Formation of protein structure 10. Multidomain Proteins 10.1. Criterion of Cooperativity 10.2. Proteins with internal homology 11. Macromolecular complexes 11.1. Entropy of association reaction 11.2. Calorimetry of association entropy 11.3. Thermodynamics of molecular recognition 12. Protein-DNA Interaction 12.1. Problems 12.2. Binding to the major groove of DNA 12.3. Binding to the minor groove of DNA 12.4. Comparative analysis of protein-DNA complexes. 12.5. Concluding remarks 13. Nucleic acids 13. 1. DNA 13.2. Polynucleotides 13.3. Short DNA duplexes 13.4. RNA
Autoren-Porträt von Peter L. Privalov
PETER L. PRIVALOV is a Professor of Biology and Biophysics at the Johns Hopkins University since 1991. He received his PhD in physics from the University of Georgia, Tbilisi (former USSR), and his DrSc in biophysics from the Institute of Biophysics, Russian Academy of Sciences, Moscow. For many years, he headed the Laboratory of Thermodynamics at the Protein Research Institute of the Russian Academy of Sciences. He is the author of 230 scientific papers published in various international journals and periodicals.
Bibliographische Angaben
- Autor: Peter L. Privalov
- 2012, 1. Auflage, 404 Seiten, Englisch
- Verlag: John Wiley & Sons
- ISBN-10: 1118337476
- ISBN-13: 9781118337479
- Erscheinungsdatum: 29.05.2012
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