Microcalorimetry of Macromolecules - The Physical Basis of Biological Structures

Informationen zum Autor 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. Klappentext Examining the physical basis of the structure of macromolecules--proteins, nucleic acids, and their complexes--using calorimetric techniquesMany 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 interactThe 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. Zusammenfassung 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. Inhaltsverzeichnis 1 Introduction 1 2 Methodology 5 2.1 Thermodynamic Basics of Calorimetry 5 2.1.1 Energy 5 2.1.2 Enthalpy 6 2.1.3 Temperature 6 2.1.4 Energy Units 7 2.1.5 Heat Capacity 8 2.1.6 Kirchhoff's Relation 9 2.1.7 Entropy 11 2.1.8 Gibbs Free Energy 13 2.2 Equilibrium Analysis 13 2.2.1 Two-State Transition 13 2.2.2 Derivatives of the Equilibrium Constant 15 2.3 Aqueous Solutions 16 2.3.1 Specifi city of Water as a Solvent 16 2.3.2 Acid-Base Equilibrium 18 2.3.3 Partial Quantities 20 2.4 Transfer of Solutes into the Aqueous Phase 23<...

List of contents

1 Introduction 1
 
2 Methodology 5
 
2.1 Thermodynamic Basics of Calorimetry, 5
 
2.1.1 Energy, 5
 
2.1.2 Enthalpy, 6
 
2.1.3 Temperature, 6
 
2.1.4 Energy Units, 7
 
2.1.5 Heat Capacity, 8
 
2.1.6 Kirchhoff's Relation, 9
 
2.1.7 Entropy, 11
 
2.1.8 Gibbs Free Energy, 13
 
2.2 Equilibrium Analysis, 13
 
2.2.1 Two-State Transition, 13
 
2.2.2 Derivatives of the Equilibrium Constant, 15
 
2.3 Aqueous Solutions, 16
 
2.3.1 Specifi city of Water as a Solvent, 16
 
2.3.2 Acid-Base Equilibrium, 18
 
2.3.3 Partial Quantities, 20
 
2.4 Transfer of Solutes into the Aqueous Phase, 23
 
2.4.1 Hydration Effects, 23
 
2.4.2 Hydrophobic Force, 25
 
2.4.3 Hydration of Polar and Nonpolar Groups, 28
 
References, 32
 
3 Calorimetry 33
 
3.1 Isothermal Reaction Microcalorimetry, 33
 
3.1.1 The Heat of Mixing Reaction, 33
 
3.1.2 Mixing of Reagents in Comparable Volumes, 35
 
3.1.3 Isothermal Titration Microcalorimeter, 36
 
3.1.4 ITC Experiments, 38
 
3.1.5 Analysis of the ITC Data, 41
 
3.2 Heat Capacity Calorimetry, 43
 
3.2.1 Technical Problems, 43
 
3.2.2 Differential Scanning Microcalorimeter, 44
 
3.2.3 Determination of the Partial Heat Capacity of Solute Molecules, 53
 
3.2.4 DSC Experiments, 55
 
3.2.5 Determination of the Enthalpy of a Temperature-Induced Process, 56
 
3.2.6 Determination of the van't Hoff Enthalpy, 58
 
3.2.7 Multimolecular Two-State Transition, 59
 
3.2.8 Analysis of the Complex Heat Capacity Profile, 60
 
3.2.9 Correction for Components Refolding, 61
 
3.3 Pressure Perturbation Calorimetry, 63
 
3.3.1 Heat Effect of Changing Pressure, 63
 
3.3.2 Pressure Perturbation Experiment, 65
 
References, 67
 
4 Macromolecules 69
 
4.1 Evolution of the Concept, 69
 
4.2 Proteins, 71
 
4.2.1 Chemical Structure, 71
 
4.2.2 Physical Structure, 76
 
4.2.3 Restrictions on the Conformation of Polypeptide Chains, 81
 
4.2.4 Regular Conformations of Polypeptide Chain Proteins, 82
 
4.3 Hierarchy in Protein Structure, 86
 
4.3.1 Tertiary Structure of Proteins, 86
 
4.3.2 Quaternary Structure of Proteins, 88
 
4.4 Nucleic Acids, 89
 
4.4.1 Chemical Structure, 89
 
4.4.2 Physical Structure, 91
 

References, 94
 
5 The alpha-Helix and alpha-Helical Coiled-Coil 95
 
5.1 The alpha-Helix, 95
 
5.1.1 Calorimetric Studies of alpha-Helix Unfolding-Refolding, 95
 
5.1.2 Analysis of the Heat Capacity Function, 99
 
5.2 alpha-Helical Coiled-Coils, 105
 
5.2.1 Two-Stranded Coiled-Coils, 105
 
5.2.2 Three-Stranded Coiled-Coils, 110
 
5.3 alpha-Helical Coiled-Coil Proteins, 113
 
5.3.1 Muscle Proteins, 113
 
5.3.2 Myosin Rod, 115
 
5.3.3 Paramyosin, 116
 
5.3.4 Tropomyosin, 117
 
5.3.5 Leucine Zipper, 118
 
5.3.6 Discreteness of the Coiled-Coils, 123
 
References, 124
 
6 Polyproline-II Coiled-Coils 127
 
6.1 Collagens, 127
 
6.1.1 Collagen Superhelix, 127
 
6.1.2 Hydrogen Bonds in Collagen, 129
 
6.1.3 Stability of Collagens, 131
 
6.1.4 Role of Pyrrolidine Rings in Collagen Stabilization, 133
 
6.2 Calorimetric Studies of Collagens, 135
 
6.2.1 Enthalpy and Entropy of Collagen Melting, 135
 
6.2.2 Correlation between Thermodynamic and Structural Characteristics of Colla

Product details

• Authors: Peter L Privalov, Peter L. Privalov, Privalov Peter L.
• Publisher: Wiley, John and Sons Ltd
• Languages: English
• Product format: Hardback
• Released: 31.08.2012
• EAN: 9781118104514
• ISBN: 978-1-118-10451-4
• No. of pages: 404
• Dimensions: 165 mm x 242 mm x 27 mm
• Subjects: Natural sciences, medicine, IT, technology > Chemistry > Organic chemistry; Chemie, Physik, Biophysik, Life Sciences, Biowissenschaften, Makromolekül, chemistry, Physics, Biophysics, Biochemie u. Chemische Biologie, Biochemistry (Chemical Biology), Proteins & Macromolecules, Proteine u. Makromoleküle, Kalorimetrie