Ideas in chemistry and molecular sciences Where chemistry meets life [[electronic resource] /] / edited by Bruno Pignataro

• Record Nr.: UNINA9910140705003321
• Pubbl/distr/stampa: Weinheim, : Wiley-VCH, 2010
• ISBN: 1-283-14048-9; 9786613140487; 3-527-63051-1; 3-527-63052-X
• Edizione: [1st ed.]
• Descrizione fisica: 1 online resource (359 p.)
• Altri autori (Persone): PignataroBruno
• Disciplina: 541.22
• Soggetti: Molecular theory; Chemistry - Social aspects
• Lingua di pubblicazione: Inglese
• Formato: Materiale a stampa
• Livello bibliografico: Monografia
• Note generali: Description based upon print version of record.
• Nota di bibliografia: Includes bibliographical references and index.
• Nota di contenuto: Ideas in Chemistry and Molecular Sciences; Contents; 5.2.6.1 Streptavidin-Biotin; Preface; List of Contributors; Part I Biochemical Studies; 1 The Role of Copper Ion and the Ubiquitin System in Neurodegenerative Disorders; 1.1 Introduction; 1.2 Metal Ions in the Brain; 1.3 Brain Copper Homeostasis; 1.4 Brain Copper and Neurodegenerative Disorders; 1.5 The Role of Ubiquitin in Protein Degradation; 1.6 Failure of the Ubiquitin System in Neurodegenerative Disorders; 1.7 Interaction of Ubiquitin with Metal Ions; 1.7.1 Thermal Stability of Ubiquitin; 1.7.2 Spectroscopic Characterization of CuII Binding1.7.3 Possible Implications for the Polyubiquitination Process; 1.7.4 CuII-Induced Self-Oligomerization of Ub; 1.7.5 Cooperativity between CuII-Binding and Solvent Polarity; 1.7.6 Comparison with Other Metal Ions; 1.8 Biological Implications; 1.8.1 The Redox State of Cellular Copper; 1.8.2 Ubiquitin and Phospholipids; 1.9 Conclusions and Perspectives; Acknowledgments; References; 2 The Bioinorganic and Organometallic Chemistry of Copper(III); 2.1 Introduction; 2.2 Bioinorganic Implications of Copper(III); 2.2.1 Dinuclear Type-3 Copper Enzymes2.2.2 Particulate Methano ; Monooxygenase (pMMO); 2.2.3 Mononuclear Monooxygenating Copper-based Enzymes; 2.2.4 Trinuclear Copper Models for Laccase; 2.3 Organometallic CuIII Species in Organic Transformations; 2.3.1 C-C Bond Formation in Organocuprate(I) Catalysis; 2.3.1.1 Conjugate Addition to α-Enones; 2.3.1.2 Acetylene Carbocupration; 2.3.1.3 SN2 and SN2 Alkylations; 2.3.2 Aryl-Heteroatom Bond Formation in Cu-mediated Cross-coupling Processes; 2.3.3 Aromatic and Aliphatic C-H Bond Organometallic Functionalizations; 2.3.3.1 Catalytic Systems; 2.3.3.2 Stoichiometric Systems2.4 Miscellany: Cuprate Superconducting Materials; 2.5 Overview and Future Targets; References; 3 Chemical Protein Modi.cation; 3.1 Introducing Diversity by Posttranslational Modification; 3.2 Chemistry: A Route to Modi.ed Proteins; 3.3 Challenges in Chemical Protein Modification; 3.4 Traditional Methods for Protein Modification; 3.4.1 Lysine Modi.cation; 3.4.1.1 Activated Esters; 3.4.1.2 Isocyanates and Isothiocyanates; 3.4.1.3 Reductive Alkylation; 3.4.1.4 IME Reagents; 3.4.2 Glutamic and Aspartic Acid Modification; 3.4.3 Cysteine; 3.4.3.1 Alkylation; 3.4.3.2 Disulfides3.4.3.3 Desulfurization at Cysteine; 3.5 Recent Innovations in Site-Selective Protein Modification; 3.5.1 Dehydroalanine: A Useful Chemical Handle for Protein Conjugation; 3.5.2 Metal-Mediated Protein Modification; 3.5.2.1 Modification at Natural Residues; 3.5.2.2 Iridium-Catalyzed Reductive Alkylation of Lysine; 3.5.2.3 Modification of Unnatural Residues; 3.5.2.4 Olefin Metathesis at S-Allyl Cysteine; 3.5.3 Metal-Free Methods for Modifying Unnatural Amino Acids; 3.5.3.1 Oxime Ligation at Aldehydes and Ketones; 3.5.3.2 Azide and Alkyne Modification; 3.5.3.3 Selective Modification of Tetrazole-Containing Proteins
• Sommario/riassunto: Ideas in Chemistry and Molecular Sciences gives an account of the most recent results of research in life sciences in Europe based on a selection of leading young scientists participating in the 2008 European Young Chemists Award competition. In addition to this, the authors provide the state of the art of their field of research and the perspective or preview of future directions.