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<p>Preface xi</p> <p><b>1 Historical Perspective 1</b></p> <p>1.1 Biomineralization 1</p> <p>1.2 Coagulation 4</p> <p>1.3 Secondary Messengers (Anticipated) 6</p> <p>1.4 Colloids 6</p> <p>1.5 Cross-Linking and Cell Surfaces 8</p> <p>1.6 Secondary Messengers (Updated) 10</p> <p>1.7 Pumps Channels and Ionophores 12</p> <p>1.8 Calcium Binding Proteins 1</p> <p>1.9 Secondary Messengers (Yet Again) 14</p> <p>1.10 Mitochondria 16</p> <p>1.11 Pumps Channels and Ionophores 18</p> <p>1.12 Hormones 23</p> <p>1.13 Measurement 26</p> <p>1.14 Biomineralization: Redux 29</p> <p><b>2 Physiological Processes Involving Calcium Binding Proteins 33</b></p> <p>2.1 Calcium as a Secondary Messenger 34</p> <p>2.2 Calcium Buffers 41</p> <p>2.3 Calcium Pumps and Channels 41</p> <p>2.4 Mitochondria 42</p> <p>2.5 Eubacteria 43</p> <p>2.6 Calcium and Extracellular Proteins 45</p> <p>2.7 Biomineralization 46</p> <p>2.8 Calcium and Viruses 51</p> <p><b>3 Comparison of the Ca 2+ Ion with Other Metal Cations 55</b></p> <p>3.1 Calcium Isotopes 55</p> <p>3.2 Calcium in the Environment 55</p> <p>3.3 Uses of Calcium 56</p> <p>3.4 Health Effects of Calcium 57</p> <p>3.5 Biologically Significant Metals in the Periodic Table 57</p> <p>3.6 Hydration of Metal Ions 59</p> <p>3.7 “Hard” and “Soft” Metal Ions 60</p> <p><b>4 Complexes of Calcium and Other Cations with Compounds of Low Molecular Weight 63</b></p> <p>4.1 Crystal Structures of Complexes of Calcium with Low Molecular Weight Compounds 63</p> <p>4.2 Dissociation Constants of Calcium and Analogs with Small Compounds 66</p> <p>4.3 Solubilities of Calcium and Analogs with Small Compounds 67</p> <p><b>5 Stoichiometry Kinetics and Thermodynamics of Calcium Binding 71</b></p> <p>5.1 Stoichiometry Affinity and Cooperativity of Binding 71</p> <p>5.2 Kinetics of Binding 77</p> <p>5.3 Partition of Free Energy of Binding (�G) Among Enthalpy (�H) and Entropy (�S) 78</p> <p><b>6 Experimental Methods Used to Study Calcium Binding to Proteins 83</b></p> <p>6.1 Radioactivity 83</p> <p>6.2 Ion-Selective Electrodes 84</p> <p>6.3 Calcium Buffers 85</p> <p>6.4 Dialysis Equilibrium and Flow 86</p> <p>6.5 Proteolysis 88</p> <p>6.6 Deuterium Exchange 88</p> <p>6.7 Isothermal Titration Calorimetry 89</p> <p>6.8 Differential Scanning Calorimetry 91</p> <p>6.9 Mass Spectroscopy 92</p> <p>6.10 Calcium-Specific Dyes and Fluors 94</p> <p>6.11 Atomic Flame Absorption Spectroscopy 97</p> <p>6.12 Absorption Spectroscopy 99</p> <p>6.13 Fluorescence Spectroscopy 102</p> <p>6.14 Circular Dichroic and Optical Rotatory Dispersion Spectroscopy 105</p> <p>6.15 Nuclear Magnetic Resonance 107</p> <p>6.16 Electron Spin Resonance 110</p> <p>6.17 Surface Plasmon Resonance 111</p> <p>6.18 Extended X-ray Absorption Spectroscopy 112</p> <p>6.19 Small Angle X-ray Scattering 113</p> <p>6.20 Crystallography 113</p> <p><b>7 Structure and Evolution of Proteins 117</b></p> <p>7.1 Domain 117</p> <p>7.2 Structure 119</p> <p>7.3 Evolution 122</p> <p><b>8 Protein Complexes with Metals Other than Calcium 127</b></p> <p>8.1 Essential Hard Cations 129</p> <p>8.2 Essential Metals with Several Valence States 152</p> <p>8.3 Conclusions 187</p> <p><b>9 Nonessential Metals 189</b></p> <p>9.1 Alkali Metals (Group Ia) 189</p> <p>9.2 Alkali Earth Metals (Group IIa) 193</p> <p>9.3 Group IIIa 197</p> <p>9.4 Group IVa 204</p> <p>9.5 Group Va 206</p> <p>9.6 Group VIIa 206</p> <p>9.7 Group VIII 207</p> <p>9.8 Group Ib 209</p> <p>9.9 Mercury (Group IIb) 210</p> <p>9.10 Group IIIb 211</p> <p>9.11 Group IVb 215</p> <p>9.12 Group Vb 217</p> <p>9.13 Polonium (Group VIb) 219</p> <p>9.14 Conclusions and Generalizations 219</p> <p><b>10 Parvalbumin 221</b></p> <p>10.1 Structure 221</p> <p>10.2 Function 231</p> <p><b>11 EF-Hand Proteins 237</b></p> <p>11.1 CTER (Calmodulin Troponin C Essential and Regulatory Light Chain) Subfamily 237</p> <p>11.2 CPR (Calcineurin B p22 Recoverin) Subfamily 266</p> <p>11.3 S100 Subfamily 278</p> <p>11.4 Penta-EF-Hand Subfamily 294</p> <p>11.5 Proteins with Six EF-Hands 300</p> <p>11.6 Proteins with Eight and 12 EF-Hands 305</p> <p>11.7 Proteins with Four EF-Hands 306</p> <p>11.8 Proteins with Two EF-Hands 315</p> <p>11.9 EF-Hand Proteins in Bacteria and Viruses 323</p> <p><b>12 Cytosolic Calcium Binding Proteins Lacking EF-Hands 327</b></p> <p>12.1 Annexins 328</p> <p>12.2 C2-Domain Proteins 334</p> <p>12.3 Calcium ATPases 350</p> <p>12.4 Calcium Binding Proteins of the Endoplasmic Reticulum 354</p> <p><b>13 Extracellular Calcium Binding Proteins 361</b></p> <p>13.1 α-Lactalbumin 362</p> <p>13.2 Cell Matrix Proteins 371</p> <p>13.3 Blood-Clotting Proteins 380</p> <p>13.4 Osteocalcin 383</p> <p>13.5 Calcium Binding Lectins 385</p> <p>13.6 Calcium Binding Hydrolytic Enzymes 389</p> <p>13.7 Miscellaneous 396</p> <p><b>14 Interactions of Calcium Binding Proteins with Other Metal Ions 399</b></p> <p>14.1 Magnesium 399</p> <p>14.2 Sodium and Potassium 402</p> <p>14.3 Zinc 403</p> <p>14.4 Trace Metals 406</p> <p><b>15 Interactions of Calcium Binding Proteins with Other Proteins and with Membranes 411</b></p> <p>15.1 Interactions with Other Proteins 411</p> <p>15.2 Interactions with Membranes 428</p> <p><b>16 Genetic Engineering of Calcium Binding Proteins 439</b></p> <p>16.1 Problems 440</p> <p>16.2 Insertion of Reporter Groups 441</p> <p>16.3 Mutations in Calcium Binding Sites 442</p> <p>16.4 Mutations Elsewhere Than in Calcium Binding Sites 448</p> <p>16.5 Generation of Chimeric Proteins 451</p> <p>16.6 Creation of Calcium Binding Sites in Proteins 453</p> <p>16.7 Studies of Protein–Protein and Protein–Membrane Interactions 455</p> <p>References 459</p> <p>Index 567</p>

<b>Eugene A. Permyakov</b> received his PhD in physics and mathematics at the Moscow Institute of Physics and Technology in 1976 and defended his Doctor of Science dissertation in biology at Moscow State University in 1989. From 1970 to 1994, he worked at the Institute of Theoretical and Experimental Bio-physics of the Russian Academy of Sciences. Since 1994 he has been the Director of the Institute for Biological Instrumentation of the Russian Academy of Sciences. He is known for his work on metal binding proteins and the intrinsic fluorescence method. His primary research focus is the study of physico-chemical and functional properties of metal binding (especially calcium-binding) proteins. <p><b>Robert H. Kretsinger</b> received his PhD in biophysics at the Massachusetts Institute of Technology under the supervision of Alex Rich in 1964. In 1967 he set up a protein crystallography lab in the Department of Biology at the University of Virginia, where he¿presently teaches, and determined the crystal structure of parvalbumin as well as describing the EF-hand domain in 1971. He has subsequently investigated the structures, functions, and evolution of various EF-hand homologs, along with other protein families. From 1978 to 1995, he directed a national facility to build multiwire area detectors for x-ray diffraction and to collect data from protein crystals.</p>

An up-to-date exploration on the latest developments in all the major families of calcium binding proteins <p>Playing a prominent role as a signal transducer, calcium is an important participant in the communication pipeline directing cellular activity. This expert guide explains the unique and highly diverse functions of calcium in biology, culminating with a discussion of the calcium binding proteins that act as secondary messengers in cells and are responsible in controlling vital bodily mechanisms such as muscle contraction and the regulation of enzymes.</p> <p>A comprehensive volume reflecting breakthrough science, <i>Calcium Binding Proteins</i>:</p> <ul> <li> <p>Contains current information on all major families of calcium binding proteins including their structural, physico-chemical and functional properties, as well as their evolution</p> </li> <li> <p>Discusses techniques that underlie the description of proteins, including NMR, circular dichroism, optical rotatory dispersion spectroscopy, calorimetry, and crystallography</p> </li> <li> <p>Describes the structures, physical characteristics, functions, and general patterns in the evolution of calcium binding proteins</p> </li> </ul> <p>This book relies on the most current biological findings to cover the patterns of biochemical phenomena such as calcium homeostasis, min-eralization, and cell signaling involving specific proteins. Summarizing ongoing studies and presenting general hypotheses that help to focus future research, Calcium Binding Proteins provides newcomers to this field as well as established professionals with a conceptual framework instru-mental in advancing their scientific pursuits.</p>

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