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E-Book, Englisch, 404 Seiten, E-Book

Privalov Microcalorimetry of Macromolecules

The Physical Basis of Biological Structures
1. Auflage 2012
ISBN: 978-1-118-33747-9
Verlag: John Wiley & Sons
Format: PDF
Kopierschutz: Adobe DRM (»Systemvoraussetzungen)

The Physical Basis of Biological Structures

E-Book, Englisch, 404 Seiten, E-Book

ISBN: 978-1-118-33747-9
Verlag: John Wiley & Sons
Format: PDF
Kopierschutz: Adobe DRM (»Systemvoraussetzungen)



Examining the physical basis of the structure ofmacromolecules--proteins, nucleic acids, and theircomplexes--using calorimetric techniques
Many scientists working in biology are unfamiliar with thebasics of thermodynamics and its role in determining molecularstructures. Yet measuring the heat of structural change a moleculeundergoes under various conditions yields information on theenergies involved and, thus, on the physical bases of theconsidered structures. Microcalorimetry of Macromoleculesoffers protein scientists unique access to this importantinformation.
Divided into thirteen chapters, the book introduces readers tothe basics of thermodynamics as it applies to calorimetry, theevolution of the calorimetric technique, as well as howcalorimetric techniques are used in the thermodynamic studies ofmacromolecules, detailing instruments for measuring the heateffects of various processes. Also provided is general informationon the structure of biological macromolecules, proteins, andnucleic acids, focusing on the key thermodynamic problems relatingto their structure. The book covers:
* The use of supersensitive calorimetric instruments, includingmicro and nano-calorimeters for measuring the heat of isothermalreactions (Isothermal Titration Nano-Calorimeter), the heatcapacities over a broad temperature range (ScanningNano-Calorimeter), and pressure effects (Pressure PerturbationNano-Calorimeter)
* Two of the simplest but key structural elements: the alpha andpolyproline helices and their complexes, the alpha-helicalcoiled-coil, and the pyroline coiled-coils
* Complicated macromolecular formations, including small globularproteins, multidomain proteins and their complexes, and nucleicacids
* Numerous examples of measuring the ground state of proteinenergetics, as well as changes seen when proteins interact
The book also reveals how intertwined structure andthermodynamics are in terms of a macromolecule's organization,mechanism of formation, the stabilization of its three-dimensionalstructure, and ultimately, its function. The first book to describemicrocalorimetric technique in detail, enough for graduate studentsand research scientists to successfully plumb the structuralmysteries of proteins and the double helix, Microcalorimetry ofMacromolecules is an essential introduction to using amicrocalorimeter in biological studies.

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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


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.



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