Microcalorimetry of Macromolecules :The Physical Basis of Biological Structures

Publication subTitle :The Physical Basis of Biological Structures

Author: Peter L. Privalov  

Publisher: John Wiley & Sons Inc‎

Publication year: 2012

E-ISBN: 9781118337479

P-ISBN(Hardback):  9781118104514

Subject: Q71 structure and function of biological macromolecules

Language: ENG

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Description

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.

Chapter

CONTENTS

pp.:  1 – 7

1: INTRODUCTION

pp.:  7 – 13

2: METHODOLOGY

pp.:  13 – 17

3: CALORIMETRY

pp.:  17 – 45

4: MACROMOLECULES

pp.:  45 – 81

5: THE α-HELIX AND α-HELICAL COILED-COIL

pp.:  81 – 107

6: POLYPROLINE-II COILED-COILS

pp.:  107 – 139

7: GLOBULAR PROTEINS

pp.:  139 – 165

8: ENERGETIC BASIS OF PROTEIN STRUCTURE

pp.:  165 – 205

9: PROTEIN FOLDING

pp.:  205 – 237

10: MULTIDOMAIN PROTEINS

pp.:  237 – 261

11: MACROMOLECULAR COMPLEXES

pp.:  261 – 285

12: PROTEIN–DNA INTERACTION

pp.:  285 – 309

13: NUCLEIC ACIDS

pp.:  309 – 365

INDEX

pp.:  365 – 399

LastPages

pp.:  399 – 422

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