{"product_id":"chemical-ligation-isbn-9781119044109","title":"Chemical Ligation","description":"Presenting a wide array of information on chemical ligation – one of the more powerful tools for protein and peptide synthesis – this book helps readers understand key methodologies and applications that protein therapeutic synthesis, drug discovery, and molecular imaging.\u003cbr\u003e\u003cbr\u003e•    Moves from fundamental to applied aspects, so that novice readers can follow the entire book and apply these reactions in the lab\u003cbr\u003e•    Presents a wide array of information on chemical ligation reactions, otherwise scattered across the literature, into one source\u003cbr\u003e•    Features comprehensive and multidisciplinary coverage that goes from basics to advanced topics\u003cbr\u003e•    Helps researchers choose the right chemical ligation technique for their needs \u003cp\u003eList of Figures xiii\u003c\/p\u003e \u003cp\u003eList of Plates xxiii\u003c\/p\u003e \u003cp\u003eList of Contributors xxix\u003c\/p\u003e \u003cp\u003ePreface xxxiii\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 Introduction to Chemical Ligation Reactions 1\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eLucia De Rosa, Alessandra Romanelli, and Luca Domenico D’Andrea\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e1.1 Introduction 1\u003c\/p\u003e \u003cp\u003e1.1.1 Chemical Synthesis of Proteins: From the Stepwise Synthesis to the Chemical Ligation Approach 2\u003c\/p\u003e \u003cp\u003e1.1.2 Chemical Modification of Proteins: From Conventional Methods to Chemoselective Labeling by Chemical Ligation 5\u003c\/p\u003e \u003cp\u003e1.2 Chemical Ligation Chemistries 6\u003c\/p\u003e \u003cp\u003e1.3 Imine Ligations 7\u003c\/p\u003e \u003cp\u003e1.3.1 Oxime Ligation 7\u003c\/p\u003e \u003cp\u003e1.3.2 Hydrazone Ligation 13\u003c\/p\u003e \u003cp\u003e1.3.3 Pictet–Spengler Ligation 15\u003c\/p\u003e \u003cp\u003e1.3.4 Thiazolidine Ligation 19\u003c\/p\u003e \u003cp\u003e1.4 Serine\/Threonine Ligation (STL) 21\u003c\/p\u003e \u003cp\u003e1.5 Thioether Ligation 24\u003c\/p\u003e \u003cp\u003e1.6 Thioester Ligation 25\u003c\/p\u003e \u003cp\u003e1.6.1 Native Chemical Ligation (NCL) 26\u003c\/p\u003e \u003cp\u003e1.6.2 Expressed Protein Ligation (EPL) 40\u003c\/p\u003e \u003cp\u003e1.6.2.1 Protein trans‐Splicing (PTS) 43\u003c\/p\u003e \u003cp\u003e1.6.3 Thioacid‐Mediated Ligation Strategies 44\u003c\/p\u003e \u003cp\u003e1.7 α‐Ketoacid‐Hydroxylamine (KAHA) Ligation 49\u003c\/p\u003e \u003cp\u003e1.7.1 Acyltrifluoroborates and Hydroxylamines Ligation 51\u003c\/p\u003e \u003cp\u003e1.8 Staudinger Ligation 52\u003c\/p\u003e \u003cp\u003e1.9 Azide–Alkyne Cycloaddition 57\u003c\/p\u003e \u003cp\u003e1.10 Diels–Alder Ligation 61\u003c\/p\u003e \u003cp\u003eReferences 64\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 Protein Chemical Synthesis by SEA Ligation 89\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eOleg Melnyk, Claire Simonneau, and Jérôme Vicogne\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e2.1 Introduction 89\u003c\/p\u003e \u003cp\u003e2.2 Essential Chemical Properties of SEA Group 93\u003c\/p\u003e \u003cp\u003e2.3 Protein Total Synthesis Using SEA Chemistry – SEA\u003csup\u003eon\/off\u003c\/sup\u003e Concept 97\u003c\/p\u003e \u003cp\u003e2.3.1 Synthesis of SEA off Peptide Segments 97\u003c\/p\u003e \u003cp\u003e2.3.2 SEA\u003csup\u003eon\/off\u003c\/sup\u003e Concept and the Design of a One-Pot Three Peptide Segment Assembly Process 99\u003c\/p\u003e \u003cp\u003e2.3.3 SEA\u003csup\u003eon\/off\u003c\/sup\u003e Concept and the Solid-Phase Synthesis of Proteins in the N-to-C Direction 103\u003c\/p\u003e \u003cp\u003e2.4 Chemical Synthesis of HGF\/SF Subdomains for Deciphering the Functioning of HGF\/SF-MET System 106\u003c\/p\u003e \u003cp\u003e2.5 Conclusion 114\u003c\/p\u003e \u003cp\u003eReferences 114\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 Development of Serine\/Threonine Ligation and Its Applications 125\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eTianlu li and Xuechen li\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e3.1 Introduction 125\u003c\/p\u003e \u003cp\u003e3.1.1 Protein Synthesis by SPPS 125\u003c\/p\u003e \u003cp\u003e3.1.2 Native Chemical Ligation (and Extended Desulfurization) 125\u003c\/p\u003e \u003cp\u003e3.1.3 KAHA Ligation 128\u003c\/p\u003e \u003cp\u003e3.2 Serine\/Threonine Ligation (STL) 130\u003c\/p\u003e \u003cp\u003e3.2.1 SAL Ester Preparation 130\u003c\/p\u003e \u003cp\u003e3.2.2 N‐Terminal‐Protecting Group for Successive C‐to‐N Ser\/Thr Ligations 136\u003c\/p\u003e \u003cp\u003e3.2.3 Scope and Limitations 137\u003c\/p\u003e \u003cp\u003e3.2.3.1 Effect of Side‐Chain‐Unprotected Lys Residue 137\u003c\/p\u003e \u003cp\u003e3.2.3.2 Effect of the C‐Terminal Amino Acid at Ligation Site 138\u003c\/p\u003e \u003cp\u003e3.3 Application of STL in Protein Synthesis 140\u003c\/p\u003e \u003cp\u003e3.3.1 Consecutive STL of Peptides\/Proteins 140\u003c\/p\u003e \u003cp\u003e3.3.1.1 Teriparatide (Forteo) 140\u003c\/p\u003e \u003cp\u003e3.3.1.2 hGH‐RH 141\u003c\/p\u003e \u003cp\u003e3.3.1.3 Human Erythrocyte Acylphosphatase (ACYP1) 142\u003c\/p\u003e \u003cp\u003e3.3.1.4 MUC1 Glycopeptides 143\u003c\/p\u003e \u003cp\u003e3.3.2 STL‐Mediated Peptide Cyclization 143\u003c\/p\u003e \u003cp\u003e3.3.2.1 STL in Head‐to‐Tail Tetrapeptide Cyclization 143\u003c\/p\u003e \u003cp\u003e3.3.2.2 STL in Head‐to‐Tail Cyclization of Peptides of Various Sizes 145\u003c\/p\u003e \u003cp\u003e3.3.2.3 Total Synthesis of Daptomycin via Serine‐Ligation‐Mediated Peptide Cyclization 145\u003c\/p\u003e \u003cp\u003e3.3.3 Thiol SAL Ester‐Mediated Aminolysis in Peptide Cyclization 147\u003c\/p\u003e \u003cp\u003e3.3.4 A Fluorogenic Probe for Recognizing 5‐OH‐Lys Inspired by STL 149\u003c\/p\u003e \u003cp\u003e3.3.5 Expressed Protein Semisynthesis via Ser\/Thr Ligation 151\u003c\/p\u003e \u003cp\u003e3.4 Conclusion and Outlook 154\u003c\/p\u003e \u003cp\u003eReferences 154\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 Synthesis of Proteins by Native Chemical Ligation–Desulfurization Strategies 161\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eBhavesh Premdjee and Richard J. Payne\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e4.1 Introduction 161\u003c\/p\u003e \u003cp\u003e4.2 Ligation–Desulfurization and Early Applications 162\u003c\/p\u003e \u003cp\u003e4.2.1 Metal‐Free Desulfurization 164\u003c\/p\u003e \u003cp\u003e4.2.2 Ligation–Desulfurization toward the Synthesis of Proteins 166\u003c\/p\u003e \u003cp\u003e4.3 Beyond Native Chemical Ligation at Cysteine – The Development of Thiolated Amino Acids and Their Application in Protein Synthesis 174\u003c\/p\u003e \u003cp\u003e4.3.1 Phenylalanine 174\u003c\/p\u003e \u003cp\u003e4.3.2 Valine 178\u003c\/p\u003e \u003cp\u003e4.3.3 Lysine 179\u003c\/p\u003e \u003cp\u003e4.3.4 Threonine 188\u003c\/p\u003e \u003cp\u003e4.3.5 Leucine 188\u003c\/p\u003e \u003cp\u003e4.3.6 Proline 193\u003c\/p\u003e \u003cp\u003e4.3.7 Glutamine 195\u003c\/p\u003e \u003cp\u003e4.3.8 Arginine 198\u003c\/p\u003e \u003cp\u003e4.3.9 Aspartic Acid 198\u003c\/p\u003e \u003cp\u003e4.3.10 Glutamic Acid 202\u003c\/p\u003e \u003cp\u003e4.3.11 Tryptophan 206\u003c\/p\u003e \u003cp\u003e4.3.12 GlcNAc‐Asparagine 206\u003c\/p\u003e \u003cp\u003e4.3.13 Asparagine 206\u003c\/p\u003e \u003cp\u003e4.4 Ligation–Deselenization in the Chemical Synthesis of Proteins 211\u003c\/p\u003e \u003cp\u003e4.4.1 Selenol Amino Acids 214\u003c\/p\u003e \u003cp\u003e4.5 Conclusions and Future Directions 216\u003c\/p\u003e \u003cp\u003eReferences 218\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 Synthesis of Chemokines by Chemical Ligation 223\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eNydia Panitz and Annette G. Beck‐Sickinger\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e5.1 Introduction – The Chemokine–Chemokine Receptor Multifunctional System 223\u003c\/p\u003e \u003cp\u003e5.2 Synthesis of Chemokines by Native Chemical Ligation 224\u003c\/p\u003e \u003cp\u003e5.3 Synthesis of Chemokines by Alternative Chemical Ligation 231\u003c\/p\u003e \u003cp\u003e5.4 Semisynthesis of Chemokines by Expressed Protein Ligation 233\u003c\/p\u003e \u003cp\u003e5.5 Prospects 241\u003c\/p\u003e \u003cp\u003eReferences 243\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6 Chemical Synthesis of Glycoproteins by the Thioester Method 251\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eHironobu Hojo\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.1 Introduction 251\u003c\/p\u003e \u003cp\u003e6.2 Ligation Methods and Strategy of Glycoprotein Synthesis 252\u003c\/p\u003e \u003cp\u003e6.3 The Synthesis of the Extracellular Ig Domain of Emmprin 254\u003c\/p\u003e \u003cp\u003e6.4 Synthesis of Basal Structure of MUC 2 256\u003c\/p\u003e \u003cp\u003e6.5 N‐Alkylcysteine‐Assisted Thioesterification Method and Dendrimer Synthesis 257\u003c\/p\u003e \u003cp\u003e6.6 Synthesis of TIM‐3 260\u003c\/p\u003e \u003cp\u003e6.7 Resynthesis of Emmprin Ig Domain 262\u003c\/p\u003e \u003cp\u003e6.8 Conclusion 264\u003c\/p\u003e \u003cp\u003eReferences 264\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 Membrane Proteins: Chemical Synthesis and Ligation 269\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eMarc Dittman and Martin Engelhard\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e7.1 Introduction 269\u003c\/p\u003e \u003cp\u003e7.2 Methods for the Synthesis and Purification of Membrane Proteins 270\u003c\/p\u003e \u003cp\u003e7.2.1 Synthesis of Hydrophobic Peptides 270\u003c\/p\u003e \u003cp\u003e7.2.2 Purification of Hydrophobic Peptides 272\u003c\/p\u003e \u003cp\u003e7.3 Ligation and Refolding 273\u003c\/p\u003e \u003cp\u003e7.3.1 Ligation Strategies 273\u003c\/p\u003e \u003cp\u003e7.3.2 Refolding of Chemically Synthesized Hydrophobic Peptides and Membrane Proteins 275\u003c\/p\u003e \u003cp\u003e7.4 Illustrative Examples 276\u003c\/p\u003e \u003cp\u003e7.4.1 Diacylglycerol Kinase (DAGK) 276\u003c\/p\u003e \u003cp\u003e7.4.2 Semisynthesis of the Sensory Rhodopsin\/Transducer Complex 278\u003c\/p\u003e \u003cp\u003e7.4.3 Semisynthesis of the Functional K + Channel KcsA 279\u003c\/p\u003e \u003cp\u003eReferences 280\u003c\/p\u003e \u003cp\u003e\u003cb\u003e8 Chemoselective Modification of Proteins 285\u003cbr\u003e \u003c\/b\u003e\u003ci\u003exi Chen, Stephanie Voss, and Yao-wen Wu\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e8.1 Chemical Protein Synthesis 285\u003c\/p\u003e \u003cp\u003e8.1.1 Native Chemical Ligation (NCL) and Expressed Protein Ligation (epl) 285\u003c\/p\u003e \u003cp\u003e8.1.2 Traceless Staudinger Ligation 286\u003c\/p\u003e \u003cp\u003e8.2 Chemoselective and Bioorthogonal Reactions 287\u003c\/p\u003e \u003cp\u003e8.2.1 Oxime\/Hydrazone Ligation 287\u003c\/p\u003e \u003cp\u003e8.2.2 Staudinger Ligations 294\u003c\/p\u003e \u003cp\u003e8.2.3 Copper-Catalyzed Azide–Alkyne Cycloaddition (CuAAC) 294\u003c\/p\u003e \u003cp\u003e8.2.4 Strain-Promoted Azide–Alkyne Cycloaddition (SPAAC) 297\u003c\/p\u003e \u003cp\u003e8.2.5 Inverse Electron-Demand Diels–Alder Cycloaddition (DA INV) 300\u003c\/p\u003e \u003cp\u003e8.2.6 Light-Induced Click Reactions 303\u003c\/p\u003e \u003cp\u003e8.2.7 1,2-Aminothiol Condensation 304\u003c\/p\u003e \u003cp\u003e8.2.8 Transition-Metal-Catalyzed Couplings 305\u003c\/p\u003e \u003cp\u003e8.2.9 Miscellaneous Protein-Labeling Reactions 306\u003c\/p\u003e \u003cp\u003e8.3 Site-Selective Protein Modification Approaches 307\u003c\/p\u003e \u003cp\u003e8.3.1 Site-Selective Modification of Native Proteins 307\u003c\/p\u003e \u003cp\u003e8.3.1.1 Cysteine (Cys), dehydroalanine (Dha), and disulfides 307\u003c\/p\u003e \u003cp\u003e8.3.1.2 N-Terminal Protein Labeling 309\u003c\/p\u003e \u003cp\u003e8.3.1.3 Kinetically-Controlled Protein Labeling (KPL) 309\u003c\/p\u003e \u003cp\u003e8.3.1.4 Affinity Labeling for Site-Specific Labeling of Native Proteins 310\u003c\/p\u003e \u003cp\u003e8.3.2 Chemical Tags for Labeling Proteins in Live Cells 311\u003c\/p\u003e \u003cp\u003e8.3.2.1 Self-Labeling Peptide Tags 312\u003c\/p\u003e \u003cp\u003e8.3.2.2 Ligand-Binding Domains 317\u003c\/p\u003e \u003cp\u003e8.3.2.3 Self-Labeling Enzymatic Domains 317\u003c\/p\u003e \u003cp\u003e8.3.2.4 Enzymatic Modifications 318\u003c\/p\u003e \u003cp\u003e8.3.2.5 Metal Chelation 318\u003c\/p\u003e \u003cp\u003e8.3.3 Unnatural Amino Acid Mutagenesis 319\u003c\/p\u003e \u003cp\u003e8.3.3.1 Residue-Specific UAA Mutagenesis Via SPI 319\u003c\/p\u003e \u003cp\u003e8.3.3.2 Site-Specific UAA Incorporation 322\u003c\/p\u003e \u003cp\u003eReferences 322\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9 Stable, Versatile Conjugation Chemistries for Modifying Aldehyde-Containing Biomolecules 339\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eAaron E. Albers, Penelope M. Drake and David Rabuka\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e9.1 Introduction 339\u003c\/p\u003e \u003cp\u003e9.2 Aldehyde as a Bioorthogonal Chemical Handle for Conjugation 339\u003c\/p\u003e \u003cp\u003e9.3 Aldehyde Conjugation Chemistries 340\u003c\/p\u003e \u003cp\u003e9.4 The Pictet–Spengler Ligation 341\u003c\/p\u003e \u003cp\u003e9.5 The Hydrazinyl-Iso-Pictet–Spengler (HIPS) Ligation 341\u003c\/p\u003e \u003cp\u003e9.6 The Trapped-Knoevenagel (thioPz) Ligation 343\u003c\/p\u003e \u003cp\u003e9.7 Applications – Antibody–Drug Conjugates 346\u003c\/p\u003e \u003cp\u003e9.8 Next-Generation HIPS Chemistry – AzaHIPS 348\u003c\/p\u003e \u003cp\u003e9.9 Applications – Protein Engineering 349\u003c\/p\u003e \u003cp\u003e9.10 Applications – Protein Labeling 349\u003c\/p\u003e \u003cp\u003e9.11 Conclusions 351\u003c\/p\u003e \u003cp\u003eReferences 351\u003c\/p\u003e \u003cp\u003e\u003cb\u003e10 Thioamide Labeling of Proteins through a Combination of Semisynthetic Methods 355\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eChristopher R. Walters, John J. Ferrie, and E. James Petersson\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e10.1 Introduction 355\u003c\/p\u003e \u003cp\u003e10.2 Thioamide Synthesis 356\u003c\/p\u003e \u003cp\u003e10.3 Thioamide Incorporation into Peptides 357\u003c\/p\u003e \u003cp\u003e10.4 Synthesis of Full‐Sized Proteins Containing Thioamides 360\u003c\/p\u003e \u003cp\u003e10.5 Applications 368\u003c\/p\u003e \u003cp\u003e10.5.1 Structural Studies 368\u003c\/p\u003e \u003cp\u003e10.5.2 Use as Photoswitches 371\u003c\/p\u003e \u003cp\u003e10.5.3 Site‐Specific Circular Dichroism Labels 373\u003c\/p\u003e \u003cp\u003e10.5.4 Fluorescence Quenching 374\u003c\/p\u003e \u003cp\u003e10.5.5 Protein Folding in Model Systems 375\u003c\/p\u003e \u003cp\u003e10.5.6 Monitoring Proteolysis 377\u003c\/p\u003e \u003cp\u003e10.5.7 α‐Synuclein Misfolding Studies 379\u003c\/p\u003e \u003cp\u003e10.6 Conclusions 381\u003c\/p\u003e \u003cp\u003eAcknowledgments 381\u003c\/p\u003e \u003cp\u003eReferences 382\u003c\/p\u003e \u003cp\u003e\u003cb\u003e11 Macrocyclic Organo-Peptide Hybrids by Intein-Mediated Ligation: Synthesis and Applications 391\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eJohn R. Frost and Rudi Fasan\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e11.1 Introduction 391\u003c\/p\u003e \u003cp\u003e11.1.1 Naturally Occurring Macrocyclic Peptides 392\u003c\/p\u003e \u003cp\u003e11.1.2 Natural Product Analogs via Reengineering of NRPS and PRPS Biosynthetic Pathways 395\u003c\/p\u003e \u003cp\u003e11.2 Macrocyclic Organo-Peptide Hybrids as Natural-Product-Inspired Macrocycles 396\u003c\/p\u003e \u003cp\u003e11.2.1 MOrPHs via CuAAC\/Hydrazide-Mediated Ligation 398\u003c\/p\u003e \u003cp\u003e11.2.2 Catalyst-Free MOrPH Synthesis via Oxime\/AMA-Mediated Ligation 401\u003c\/p\u003e \u003cp\u003e11.2.3 Structure–Reactivity Relationships in MOrPH Synthesis 401\u003c\/p\u003e \u003cp\u003e11.2.4 Synthesis of MOrPH Libraries 404\u003c\/p\u003e \u003cp\u003e11.2.5 Macrocyclization Mechanism 405\u003c\/p\u003e \u003cp\u003e11.2.6 Bicyclic Organo-Peptide Hybrids 406\u003c\/p\u003e \u003cp\u003e11.3 Application of MOrPHs for Targeting α-Helix-Mediated Protein– Protein Interactions 406\u003c\/p\u003e \u003cp\u003e11.4 Conclusions 410\u003c\/p\u003e \u003cp\u003eReferences 410\u003c\/p\u003e \u003cp\u003e\u003cb\u003e12 Protein Ligation by HINT Domains 421\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eHideo Iwaï and A. Sesilja Aranko\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e12.1 Introduction 421\u003c\/p\u003e \u003cp\u003e12.2 Protein Ligation by Protein Splicing 423\u003c\/p\u003e \u003cp\u003e12.3 Naturally Occurring and Artificially Split Inteins for Protein Ligation 424\u003c\/p\u003e \u003cp\u003e12.4 Conditional Protein Splicing 427\u003c\/p\u003e \u003cp\u003e12.5 Inter- and Intramolecular Protein Splicing 429\u003c\/p\u003e \u003cp\u003e12.6 Protein Ligation by Other HINT Domains 430\u003c\/p\u003e \u003cp\u003e12.7 Bottleneck of Protein Ligation by PTS 432\u003c\/p\u003e \u003cp\u003e12.8 Comparison with Other Enzymatic Ligation Methods 432\u003c\/p\u003e \u003cp\u003e12.9 Perspective of Protein Ligation by HINT Domains 437\u003c\/p\u003e \u003cp\u003e12.10 Conclusions and Future Perspectives 438\u003c\/p\u003e \u003cp\u003eAcknowledgment 438\u003c\/p\u003e \u003cp\u003eReferences 438\u003c\/p\u003e \u003cp\u003e\u003cb\u003e13 Chemical Ligation for Molecular Imaging 447\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eAurélien Godinat, Hacer Karatas, Ghyslain Budin, and Elena A. Dubikovskaya\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e13.1 Introduction 447\u003c\/p\u003e \u003cp\u003e13.2 Chemical Ligation 448\u003c\/p\u003e \u003cp\u003e13.2.1 Classical Chemical Ligation 448\u003c\/p\u003e \u003cp\u003e13.2.2 Bioorthogonal Chemistry 450\u003c\/p\u003e \u003cp\u003e13.2.2.1 Bioorthogonal Chemistry for Optical Imaging 454\u003c\/p\u003e \u003cp\u003e13.2.2.2 Bioorthogonal Chemistry for Nuclear Imaging (PET, SPECT) 462\u003c\/p\u003e \u003cp\u003e13.2.2.3 Bioorthogonal Chemistry for Magnetic Resonance Imaging (mri) 469\u003c\/p\u003e \u003cp\u003e13.3 Conclusion 470\u003c\/p\u003e \u003cp\u003eReferences 473\u003c\/p\u003e \u003cp\u003e\u003cb\u003e14 Native Chemical Ligation in Structural Biology 485\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eLucia De Rosa, Alessandra Romanelli, and Luca Domenico D’Andrea\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e14.1 Introduction 485\u003c\/p\u003e \u003cp\u003e14.2 Protein (Semi)synthesis for Molecular Structure Determination 486\u003c\/p\u003e \u003cp\u003e14.3 Protein (Semi)Synthesis for Understanding Protein Folding, Stability, and Interactions 494\u003c\/p\u003e \u003cp\u003e14.4 Protein (Semi)Synthesis in Enzyme Chemistry 501\u003c\/p\u003e \u003cp\u003eReferences 506\u003c\/p\u003e \u003cp\u003eIndex 517\u003c\/p\u003e   \u003cp\u003e\u003cb\u003e Luca D. D'Andrea, PhD,\u003c\/b\u003e is Research Scientist at the Institute of Biostructures and Bioimaging, CNR Naples, Italy. His scientific interests are in the field of peptide and protein chemistry. His research activity focuses on design, synthesis, and structural characterization of peptide\/proteins as therapeutic\/diagnostic agents.   \u003c\/p\u003e\u003cp\u003e\u003cb\u003e Alessandra Romanelli, PhD,\u003c\/b\u003e is assistant professor of General Chemistry at Department of Pharmacy, University of Naples \"Federico II\", Italy. She actively works in the field of peptides and peptide-based molecules (such as peptide nucleic acids) as tools for chemical biology.      \u003c\/p\u003e\u003cp\u003e Chemical biology deals with the use and development of chemical tools to solve biological problems, and chemical ligation fits within this paradigm as a set of techniques used for creating long peptide or protein chains. The practices involved represent a powerful enhancement of traditional solid-phase peptide synthesis – allowing the chemical preparation of proteins, biomolecule synthesis, protein labeling or immobilization, and preparation of proteins with unnatural amino acids. These molecular tools are useful for understanding biological systems and preparing novel bio- and nanomaterials or synthetizing bioactive molecules.   \u003c\/p\u003e\u003cp\u003e Until recently restricted to use by specialized scientists, chemical ligation methods are now in widespread use across interdisciplinary research groups and to different scientific areas. There is a clear need for a single-source resource and reference about these techniques and that is where \u003ci\u003eChemical Ligation: Tools for Biomolecule Synthesis and Modification\u003c\/i\u003e comes in.   \u003c\/p\u003e\u003cp\u003e Presenting a wide array of information on chemical ligation, this book guides readers between different chemical ligation methodologies and applications – from the basics to more recent and sophisticated applications. The chapters move from the fundamental to applied aspects, so that novice readers can follow the entire book and apply these reactions in the laboratory.   \u003c\/p\u003e\u003cp\u003e The authors reserve attention for synthetic aspects, so the book also serves as a valuable reference for experimental work. Additionally, a selection of outstanding applications – including protein therapeutic synthesis, drug discovery, and molecular imaging – provides an overview of chemical ligation's potential and get other scientists involved bringing new ideas and applications.\u003c\/p\u003e","brand":"Wiley","offers":[{"title":"Default Title","offer_id":47988906066149,"sku":"NP9781119044109","price":218.95,"currency_code":"USD","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/1842\/7735\/files\/9781119044109.jpg?v=1761781999","url":"https:\/\/k12savings.com\/products\/chemical-ligation-isbn-9781119044109","provider":"K12savings","version":"1.0","type":"link"}