{"product_id":"coordination-chemistry-in-protein-cages-9781118078570","title":"Coordination Chemistry in Protein Cages","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003e\u003cp\u003e\u003cb\u003eSets the stage for the design and application of new protein cages\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eFeaturing contributions from a team of international experts in the coordination chemistry of biological systems, this book enables readers to understand and take advantage of the fascinating internal molecular environment of protein cages. With the aid of modern organic and polymer techniques, the authors explain step by step how to design and construct a variety of protein cages. Moreover, the authors describe current applications of protein cages, setting the foundation for the development of new applications in biology, nanotechnology, synthetic chemistry, and other disciplines.\u003c\/p\u003e \u003cp\u003eBased on a thorough review of the literature as well as the authors'' own laboratory experience, \u003ci\u003eCoordination Chemistry in Protein Cages\u003c\/i\u003e\u003c\/p\u003e \u003cul\u003e \u003cli\u003eSets forth the principles of coordination reactions in natural protein cages\u003c\/li\u003e \u003cli\u003eDetails the fundamental design of coordination sites of small artificial met\u003cbr\u003e\u003cbr\u003e\u003cb\u003eTable of Contents\u003c\/b\u003e\u003cbr\u003e\u003cp\u003eForeword xiii\u003c\/p\u003e \u003cp\u003ePreface xv\u003c\/p\u003e \u003cp\u003eContributors xvii\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePART I COORDINATION CHEMISTRY IN NATIVE PROTEIN CAGES\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 The Chemistry of Nature’s Iron Biominerals in Ferritin Protein Nanocages 3\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eElizabeth C. Theil and Rabindra K. Behera\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e1.1 Introduction 3\u003c\/p\u003e \u003cp\u003e1.2 Ferritin Ion Channels and Ion Entry 6\u003c\/p\u003e \u003cp\u003e1.2.1 Maxi- and Mini-Ferritin 6\u003c\/p\u003e \u003cp\u003e1.2.2 Iron Entry 7\u003c\/p\u003e \u003cp\u003e1.3 Ferritin Catalysis 8\u003c\/p\u003e \u003cp\u003e1.3.1 Spectroscopic Characterization of -1,2 Peroxodiferric Intermediate (DFP) 8\u003c\/p\u003e \u003cp\u003e1.3.2 Kinetics of DFP Formation and Decay 12\u003c\/p\u003e \u003cp\u003e1.4 Protein-Based Ferritin Mineral Nucleation and Mineral Growth 13\u003c\/p\u003e \u003cp\u003e1.5 Iron Exit 16\u003c\/p\u003e \u003cp\u003e1.6 Synthetic Uses of Ferritin Protein Nanocages 17\u003c\/p\u003e \u003cp\u003e1.6.1 Nanomaterials Synthesized in Ferritins 18\u003c\/p\u003e \u003cp\u003e1.6.2 Ferritin Protein Cages in Metalloorganic Catalysis and Nanoelectronics 19\u003c\/p\u003e \u003cp\u003e1.6.3 Imaging and Drug Delivery Agents Produced in Ferritins 19\u003c\/p\u003e \u003cp\u003e1.7 Summary and Perspectives 20\u003c\/p\u003e \u003cp\u003eAcknowledgments 20\u003c\/p\u003e \u003cp\u003eReferences 21\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 Molecular Metal Oxides in Protein Cages\/Cavities 25\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eAchim M¨uller and Dieter Rehder\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e2.1 Introduction 25\u003c\/p\u003e \u003cp\u003e2.2 Vanadium: Functional Oligovanadates and Storage of VO2+ in Vanabins 26\u003c\/p\u003e \u003cp\u003e2.3 Molybdenum and Tungsten: Nucleation Process in a Protein Cavity 28\u003c\/p\u003e \u003cp\u003e2.4 Manganese in Photosystem II 33\u003c\/p\u003e \u003cp\u003e2.5 Iron: Ferritins, DPS Proteins, Frataxins, and Magnetite 35\u003c\/p\u003e \u003cp\u003e2.6 Some General Remarks: Oxides and Sulfides 38\u003c\/p\u003e \u003cp\u003eReferences 38\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePART II DESIGN OF METALLOPROTEIN CAGES\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 De Novo Design of Protein Cages to Accommodate Metal Cofactors 45\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eFlavia Nastri, Rosa Bruni, Ornella Maglio, and Angela Lombardi\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e3.1 Introduction 45\u003c\/p\u003e \u003cp\u003e3.2 De Novo-Designed Protein Cages Housing Mononuclear Metal Cofactors 47\u003c\/p\u003e \u003cp\u003e3.3 De Novo-Designed Protein Cages Housing Dinuclear Metal Cofactors 59\u003c\/p\u003e \u003cp\u003e3.4 De Novo-Designed Protein Cages Housing Heme Cofactor 66\u003c\/p\u003e \u003cp\u003e3.5 Summary and Perspectives 79\u003c\/p\u003e \u003cp\u003eAcknowledgments 79\u003c\/p\u003e \u003cp\u003eReferences 80\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 Generation of Functionalized Biomolecules Using Hemoprotein Matrices with Small Protein Cavities for Incorporation of Cofactors 87\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eTakashi Hayashi\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e4.1 Introduction 87\u003c\/p\u003e \u003cp\u003e4.2 Hemoprotein Reconstitution with an Artificial Metal Complex 89\u003c\/p\u003e \u003cp\u003e4.3 Modulation of the O2 Affinity of Myoglobin 90\u003c\/p\u003e \u003cp\u003e4.4 Conversion of Myoglobin into Peroxidase 95\u003c\/p\u003e \u003cp\u003e4.4.1 Construction of a Substrate-Binding Site Near the Heme Pocket 95\u003c\/p\u003e \u003cp\u003e4.4.2 Replacement of Native Heme with Iron Porphyrinoid in Myoglobin 99\u003c\/p\u003e \u003cp\u003e4.4.3 Other Systems Used in Enhancement of Peroxidase Activity of Myoglobin 100\u003c\/p\u003e \u003cp\u003e4.5 Modulation of Peroxidase Activity of HRP 102\u003c\/p\u003e \u003cp\u003e4.6 Myoglobin Reconstituted with a Schiff Base Metal Complex 103\u003c\/p\u003e \u003cp\u003e4.7 A Reductase Model Using Reconstituted Myoglobin 106\u003c\/p\u003e \u003cp\u003e4.7.1 Hydrogenation Catalyzed by Cobalt Myoglobin 106\u003c\/p\u003e \u003cp\u003e4.7.2 A Model of Hydrogenase Using the Heme Pocket of Cytochrome c 107\u003c\/p\u003e \u003cp\u003e4.8 Summary and Perspectives 108\u003c\/p\u003e \u003cp\u003eAcknowledgments 108\u003c\/p\u003e \u003cp\u003eReferences 108\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 Rational Design of Protein Cages for Alternative Enzymatic Functions 111\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eNicholas M. Marshall, Kyle D. Miner, Tiffany D. Wilson, and Yi Lu\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e5.1 Introduction 111\u003c\/p\u003e \u003cp\u003e5.2 Mononuclear Electron Transfer Cupredoxin Proteins 112\u003c\/p\u003e \u003cp\u003e5.3 CuA Proteins 116\u003c\/p\u003e \u003cp\u003e5.4 Catalytic Copper Proteins 118\u003c\/p\u003e \u003cp\u003e5.4.1 Type 2 Red Copper Sites 118\u003c\/p\u003e \u003cp\u003e5.4.2 Other T2 Copper Sites 120\u003c\/p\u003e \u003cp\u003e5.4.3 Cu, Zn Superoxide Dismutase 121\u003c\/p\u003e \u003cp\u003e5.4.4 Multicopper Oxygenases and Oxidases 122\u003c\/p\u003e \u003cp\u003e5.5 Heme-Based Enzymes 124\u003c\/p\u003e \u003cp\u003e5.5.1 Mb-Based Peroxidase and P450 Mimics 124\u003c\/p\u003e \u003cp\u003e5.5.2 Mimicking Oxidases in Mb 125\u003c\/p\u003e \u003cp\u003e5.5.3 Mimicking NOR Enzymes in Mb 127\u003c\/p\u003e \u003cp\u003e5.5.4 Engineering Peroxidase Proteins 128\u003c\/p\u003e \u003cp\u003e5.5.5 Engineering Cytochrome P450s 129\u003c\/p\u003e \u003cp\u003e5.6 Non-Heme ET Proteins 131\u003c\/p\u003e \u003cp\u003e5.7 Fe and Mn Superoxide Dismutase 132\u003c\/p\u003e \u003cp\u003e5.8 Non-Heme Fe Catalysts 133\u003c\/p\u003e \u003cp\u003e5.9 Zinc Proteins 134\u003c\/p\u003e \u003cp\u003e5.10 Other Metalloproteins 135\u003c\/p\u003e \u003cp\u003e5.10.1 Cobalt Proteins 135\u003c\/p\u003e \u003cp\u003e5.10.2 Manganese Proteins 136\u003c\/p\u003e \u003cp\u003e5.10.3 Molybdenum Proteins 137\u003c\/p\u003e \u003cp\u003e5.10.4 Nickel Proteins 137\u003c\/p\u003e \u003cp\u003e5.10.5 Uranyl Proteins 138\u003c\/p\u003e \u003cp\u003e5.10.6 Vanadium Proteins 138\u003c\/p\u003e \u003cp\u003e5.11 Summary and Perspectives 139\u003c\/p\u003e \u003cp\u003eReferences 142\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePART III COORDINATION CHEMISTRY OF PROTEIN ASSEMBLY CAGES\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6 Metal-Directed and Templated Assembly of Protein Superstructures and Cages 151\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eF. Akif Tezcan\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.1 Introduction 151\u003c\/p\u003e \u003cp\u003e6.2 Metal-Directed Protein Self-Assembly 152\u003c\/p\u003e \u003cp\u003e6.2.1 Background 152\u003c\/p\u003e \u003cp\u003e6.2.2 Design Considerations for Metal-Directed Protein Self-Assembly 153\u003c\/p\u003e \u003cp\u003e6.2.3 Interfacing Non-Natural Chelates with MDPSA 155\u003c\/p\u003e \u003cp\u003e6.2.4 Crystallographic Applications of Metal-Directed Protein Self-Assembly 159\u003c\/p\u003e \u003cp\u003e6.3 Metal-Templated Interface Redesign 162\u003c\/p\u003e \u003cp\u003e6.3.1 Background 162\u003c\/p\u003e \u003cp\u003e6.3.2 Construction of a Zn-Selective Tetrameric Protein Complex Through MeTIR 163\u003c\/p\u003e \u003cp\u003e6.3.3 Construction of a Zn-Selective Protein Dimerization Motif Through MeTIR 166\u003c\/p\u003e \u003cp\u003e6.4 Summary and Perspectives 170\u003c\/p\u003e \u003cp\u003eAcknowledgments 171\u003c\/p\u003e \u003cp\u003eReferences 171\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 Catalytic Reactions Promoted in Protein Assembly Cages 175\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eTakafumi Ueno and Satoshi Abe\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e7.1 Introduction 175\u003c\/p\u003e \u003cp\u003e7.1.1 Incorporation of Metal Compounds 176\u003c\/p\u003e \u003cp\u003e7.1.2 Insight into Accumulation Process ofMetal Compounds 177\u003c\/p\u003e \u003cp\u003e7.2 Ferritin as a Platform for Coordination Chemistry 177\u003c\/p\u003e \u003cp\u003e7.3 Catalytic Reactions in Ferritin 179\u003c\/p\u003e \u003cp\u003e7.3.1 Olefin Hydrogenation 179\u003c\/p\u003e \u003cp\u003e7.3.2 Suzuki–Miyaura Coupling Reaction in Protein Cages 182\u003c\/p\u003e \u003cp\u003e7.3.3 Polymer Synthesis in Protein Cages 185\u003c\/p\u003e \u003cp\u003e7.4 Coordination Processes in Ferritin 188\u003c\/p\u003e \u003cp\u003e7.4.1 Accumulation of Metal Ions 188\u003c\/p\u003e \u003cp\u003e7.4.2 Accumulation of Metal Complexes 192\u003c\/p\u003e \u003cp\u003e7.5 Coordination Arrangements in Designed Ferritin Cages 194\u003c\/p\u003e \u003cp\u003e7.6 Summary and Perspectives 197\u003c\/p\u003e \u003cp\u003eAcknowledgments 198\u003c\/p\u003e \u003cp\u003eReferences 198\u003c\/p\u003e \u003cp\u003e\u003cb\u003e8 Metal-Catalyzed Organic Transformations Inside a Protein Scaffold Using Artificial Metalloenzymes 203\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eV. K. K. Praneeth and Thomas R. Ward\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e8.1 Introduction 203\u003c\/p\u003e \u003cp\u003e8.2 Enantioselective Reduction Reactions Catalyzed by Artificial Metalloenzymes 204\u003c\/p\u003e \u003cp\u003e8.2.1 Asymmetric Hydrogenation 204\u003c\/p\u003e \u003cp\u003e8.2.2 Asymmetric Transfer Hydrogenation of Ketones 206\u003c\/p\u003e \u003cp\u003e8.2.3 Artificial Transfer Hydrogenation of Cyclic Imines 208\u003c\/p\u003e \u003cp\u003e8.3 Palladium-Catalyzed Allylic Alkylation 211\u003c\/p\u003e \u003cp\u003e8.4 Oxidation Reaction Catalyzed by Artificial Metalloenzymes 212\u003c\/p\u003e \u003cp\u003e8.4.1 Artificial Sulfoxidase 212\u003c\/p\u003e \u003cp\u003e8.4.2 Asymmetric cis-Dihydroxylation 215\u003c\/p\u003e \u003cp\u003e8.5 Summary and Perspectives 216\u003c\/p\u003e \u003cp\u003eReferences 218\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePART IV APPLICATIONS IN BIOLOGY\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9 Selective Labeling and Imaging of Protein Using Metal Complex 223\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eYasutaka Kurishita and Itaru Hamachi\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e9.1 Introduction 223\u003c\/p\u003e \u003cp\u003e9.2 Tag–Probe Pair Method Using Metal-Chelation System 225\u003c\/p\u003e \u003cp\u003e9.2.1 Tetracysteine Motif\/Arsenical Compounds Pair 225\u003c\/p\u003e \u003cp\u003e9.2.2 Oligo-Histidine Tag\/Ni(ii)-NTA Pair 227\u003c\/p\u003e \u003cp\u003e9.2.3 Oligo-Aspartate Tag\/Zn(ii)-DpaTyr Pair 230\u003c\/p\u003e \u003cp\u003e9.2.4 Lanthanide-binding Tag 235\u003c\/p\u003e \u003cp\u003e9.3 Summary and Perspectives 237\u003c\/p\u003e \u003cp\u003eReferences 237\u003c\/p\u003e \u003cp\u003e\u003cb\u003e10 Molecular Bioengineering of Magnetosomes for Biotechnological Applications 241\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eAtsushi Arakaki, Michiko Nemoto, and Tadashi Matsunaga\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e10.1 Introduction 241\u003c\/p\u003e \u003cp\u003e10.2 Magnetite Biomineralization Mechanism in Magnetosome 242\u003c\/p\u003e \u003cp\u003e10.2.1 Diversity of Magnetotactic Bacteria 242\u003c\/p\u003e \u003cp\u003e10.2.2 Genome and Proteome Analyses of Magnetotactic Bacteria 244\u003c\/p\u003e \u003cp\u003e10.2.3 Magnetosome Formation Mechanism 246\u003c\/p\u003e \u003cp\u003e10.2.4 Morphological Control of Magnetite Crystal in Magnetosomes 250\u003c\/p\u003e \u003cp\u003e10.3 Functional Design of Magnetosomes 251\u003c\/p\u003e \u003cp\u003e10.3.1 Protein Display on Magnetosome by Gene Fusion Technique 252\u003c\/p\u003e \u003cp\u003e10.3.2 Magnetosome Surface Modification by In Vitro System 255\u003c\/p\u003e \u003cp\u003e10.3.3 Protein-mediated Morphological Control of Magnetite Particles 257\u003c\/p\u003e \u003cp\u003e10.4 Application 258\u003c\/p\u003e \u003cp\u003e10.4.1 Enzymatic Bioassays 259\u003c\/p\u003e \u003cp\u003e10.4.2 Cell Separation 260\u003c\/p\u003e \u003cp\u003e10.4.3 DNA Extraction 262\u003c\/p\u003e \u003cp\u003e10.4.4 Bioremediation 264\u003c\/p\u003e \u003cp\u003e10.5 Summary and Perspectives 266\u003c\/p\u003e \u003cp\u003eAcknowledgments 266\u003c\/p\u003e \u003cp\u003eReferences 266\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePART V APPLICATIONS IN NANOTECHNOLOGY\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e11 Protein Cage Nanoparticles for Hybrid Inorganic–Organic Materials 275\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eShefah Qazi, Janice Lucon, Masaki Uchida, and Trevor Douglas\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e11.1 Introduction 275\u003c\/p\u003e \u003cp\u003e11.2 Biomineral Formation in Protein Cage Architectures 277\u003c\/p\u003e \u003cp\u003e11.2.1 Introduction 277\u003c\/p\u003e \u003cp\u003e11.2.2 Mineralization 278\u003c\/p\u003e \u003cp\u003e11.2.3 Model for Synthetic Nucleation-Driven Mineralization 279\u003c\/p\u003e \u003cp\u003e11.2.4 Mineralization in Dps: A 12-Subunit Protein Cage 279\u003c\/p\u003e \u003cp\u003e11.2.5 Icosahedral Protein Cages: Viruses 282\u003c\/p\u003e \u003cp\u003e11.2.6 Nucleation of Inorganic Nanoparticles Within Icosahedral Viruses 282\u003c\/p\u003e \u003cp\u003e11.3 Polymer Formation Inside Protein Cage Nanoparticles 283\u003c\/p\u003e \u003cp\u003e11.3.1 Introduction 283\u003c\/p\u003e \u003cp\u003e11.3.2 Azide–Alkyne Click Chemistry in sHsp and P22 285\u003c\/p\u003e \u003cp\u003e11.3.3 Atom Transfer Radical Polymerization in P22 287\u003c\/p\u003e \u003cp\u003e11.3.4 Application as Magnetic Resonance Imaging Contrast Agents 290\u003c\/p\u003e \u003cp\u003e11.4 Coordination Polymers in Protein Cages 292\u003c\/p\u003e \u003cp\u003e11.4.1 Introduction 292\u003c\/p\u003e \u003cp\u003e11.4.2 Metal–Organic Branched Polymer Synthesis by Preforming Complexes 292\u003c\/p\u003e \u003cp\u003e11.4.3 Coordination Polymer Formation from Ditopic Ligands and Metal Ions 295\u003c\/p\u003e \u003cp\u003e11.4.4 Altering Protein Dynamics by Coordination: Hsp-Phen-Fe 296\u003c\/p\u003e \u003cp\u003e11.5 Summary and Perspectives 298\u003c\/p\u003e \u003cp\u003eAcknowledgments 298\u003c\/p\u003e \u003cp\u003eReferences 298\u003c\/p\u003e \u003cp\u003e\u003cb\u003e12 Nanoparticles Synthesized and Delivered by Protein in the Field of Nanotechnology Applications 305\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eIchiro Yamashita, Kenji Iwahori, Bin Zheng, and Shinya Kumagai\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e12.1 Nanoparticle Synthesis in a Bio-Template 305\u003c\/p\u003e \u003cp\u003e12.1.1 NP Synthesis by Cage-Shaped Proteins for Nanoelectronic Devices and Other Applications 305\u003c\/p\u003e \u003cp\u003e12.1.2 Metal Oxide or Hydro-Oxide NP Synthesis in the Apoferritin Cavity 307\u003c\/p\u003e \u003cp\u003e12.1.3 Compound Semiconductor NP Synthesis in the Apoferritin Cavity 308\u003c\/p\u003e \u003cp\u003e12.1.4 NP Synthesis in the Apoferritin with the Metal-Binding Peptides 311\u003c\/p\u003e \u003cp\u003e12.2 Site-Directed Placement of NPs 312\u003c\/p\u003e \u003cp\u003e12.2.1 Nanopositioning of Cage-Shaped Proteins 312\u003c\/p\u003e \u003cp\u003e12.2.2 Nanopositioning of Au NPs by Porter Proteins 313\u003c\/p\u003e \u003cp\u003e12.3 Fabrication of Nanodevices by the NP and Protein Conjugates 317\u003c\/p\u003e \u003cp\u003e12.3.1 Fabrication of Floating Nanodot Gate Memory 318\u003c\/p\u003e \u003cp\u003e12.3.2 Fabrication of Single-Electron Transistor Using Ferritin 321\u003c\/p\u003e \u003cp\u003eReferences 326\u003c\/p\u003e \u003cp\u003e\u003cb\u003e13 Engineered “Cages” for Design of Nanostructured Inorganic Materials 329\u003c\/b\u003e\u003cbr\u003e \u003ci\u003ePatrick B. Dennis, Joseph M. Slocik, and Rajesh R. Naik\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e13.1 Introduction 329\u003c\/p\u003e \u003cp\u003e13.2 Metal-Binding Peptides 331\u003c\/p\u003e \u003cp\u003e13.3 Discrete Protein Cages 332\u003c\/p\u003e \u003cp\u003e13.4 Heat-Shock Proteins 334\u003c\/p\u003e \u003cp\u003e13.5 Polymeric Protein and Carbohydrate Quasi-Cages 340\u003c\/p\u003e \u003cp\u003e13.6 Summary and Perspectives 346\u003c\/p\u003e \u003cp\u003eReferences 347\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePART VI COORDINATION CHEMISTRY INSPIRED BY PROTEIN CAGES\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e14 Metal–Organic Caged Assemblies 353\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eSota Sato and Makoto Fujita\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e14.1 Introduction 353\u003c\/p\u003e \u003cp\u003e14.2 Construction of Polyhedral Skeletons by Coordination Bonds 355\u003c\/p\u003e \u003cp\u003e14.2.1 Geometrical Effect on Products 356\u003c\/p\u003e \u003cp\u003e14.2.2 Structural Extension Based on Rigid, Designable Framework 358\u003c\/p\u003e \u003cp\u003e14.2.3 Mechanistic Insight into Self-Assembly 366\u003c\/p\u003e \u003cp\u003e14.3 Development of Functions via Chemical Modification 366\u003c\/p\u003e \u003cp\u003e14.3.1 Chemistry in the Hollow of Cages 367\u003c\/p\u003e \u003cp\u003e14.3.2 Chemistry on the Periphery of Cages 368\u003c\/p\u003e \u003cp\u003e14.4 Metal–Organic Cages for Protein Encapsulation 370\u003c\/p\u003e \u003cp\u003e14.5 Summary and Perspectives 370\u003c\/p\u003e \u003cp\u003eReferences 371\u003c\/p\u003e \u003cp\u003eIndex 375\u003c\/p\u003e\n\u003c\/li\u003e\n\u003c\/ul\u003e","brand":"John Wiley \u0026 Sons Inc","offers":[{"title":"Default Title","offer_id":49406827364695,"sku":"9781118078570","price":117.85,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781118078570.jpg?v=1730497252","url":"https:\/\/bookcurl.com\/products\/coordination-chemistry-in-protein-cages-9781118078570","provider":"Book Curl","version":"1.0","type":"link"}