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Proceedings of an international conference held in Magdeburg, Germany, November 3-5, 1996.
Histology. Cytology --- General biochemistry --- Peptidase --- 577.152.34 --- Proteolytic enzymes --- Transpeptidation --- Immunology. --- Pathophysiology. --- Acting on peptide bonds (peptide hydrolases), proteolytic fermentation. Proteinases --- 577.152.34 Acting on peptide bonds (peptide hydrolases), proteolytic fermentation. Proteinases --- Immunology --- Pathophysiology --- Biochemistry. --- Biochemistry, general. --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Chemistry --- Medical sciences --- Immunobiology --- Life sciences --- Serology --- Composition
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This book presents the state of the art in the synthesis very complex saccharide structures, written by leading scientists at the forefront of this rapidly growing field. Reflecting the particular significance in recent years of efficient and selective procedures employing enzymes for preparative purposes in the carbohydrate field, a major proportion of the articles focus on these biocatalytic methods. In addition, recent strategies for the construction of unusual carbohydrates structures employing novel and creative methodologies are highlighted. Further, particular emphasis is placed on very complex saccharide structures as well as on special solutions to problems that are particularly challenging.
Carbohydrates --- Oligosaccharides --- Glycoconjugates --- Glycoconjugués --- Synthesis. --- Synthèse. --- Chemistry. --- Organic chemistry. --- Biochemistry. --- Organic Chemistry. --- Biochemistry, general. --- Glycoconjugués --- Synthèse. --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Chemistry --- Medical sciences --- Organic chemistry --- Composition --- Carbohydrates - Synthesis. --- Oligosaccharides - Synthesis. --- Glycoconjugates - Synthesis. --- OLIGOSACCHARIDES --- OLIGOSACCHARIDES, CONJUGATES --- GLYCOSIDE HYDROLASES --- LIPASES --- SIALIC ACIDS --- GLYCOSYLATION --- GLYCOPEPTIDES --- ERGOT ALKALOIDS --- PREPARATION
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Pancreatic ribonuclease, the focus of highly productive scientific research for more than half a century and the only enzyme to be the basis of four Nobel prizes, has recently undergone a resurgence in popularity for the recognition of an extended ribonuclease superfamily with functions ranging from tumour growth and inhibition to self-recognition and neurotoxicity. This volume highlights the functional diversity of ribonucleases and reveals the emerging research opportunities provided by these enzymes.* Never before has discussion of the entire family of ribonucleases and related
Nucleoproteins. --- Ribonucleases. --- Ribonucleases--Structure-activity relationships. --- RNA. --- Ribonucleases --- Structure-Activity Relationship --- Esterases --- Pharmacological Phenomena --- Biochemical Phenomena --- Hydrolases --- Physiological Phenomena --- Chemical Phenomena --- Phenomena and Processes --- Enzymes --- Enzymes and Coenzymes --- Chemicals and Drugs --- Animal Biochemistry --- Human Anatomy & Physiology --- Health & Biological Sciences --- Structure-activity relationships --- Nucleases. --- Structure-activity relationships. --- RNases --- Nucleases
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Biological chemistry is a major frontier of inorganic chemistry. Three special volumes devoted to Metal Sites in Proteins and Models address the questions: how unusual ("entatic") are metal sites in metalloproteins and metalloenzymes compared to those in small coordination complexes? and if they are special, how do polypeptide chains and co-factors control this? The chapters deal with iron, with metal centres acting as Lewis acids, metals in phosphate enzymes, with vanadium, and with the wide variety of transition metal ions which act as redox centres. They illustrate in particular how the combined armoury of genetics and structure determination at the molecular level are providing unprecedented new tools for molecular engineering.
Acides de Lewis --- Fosfatasen --- Iron proteins --- Lewis [Acides de ] --- Lewis acids --- Lewiszuren --- Metallo-enzymen --- Metalloenzymes --- Metalloproteins --- Metalloproteïnen --- Métalloenzymes --- Métalloprotéïnes --- Phosphatases --- Phosphoesterases --- Phosphohydrolases --- Vanadium --- Zuren [Lewis] --- 577.118 --- #WSCH:AAS2 --- Inorganic and mineral substances --- Metalloproteins. --- Oxidation-reduction reaction. --- 577.118 Inorganic and mineral substances --- Boranes --- Hydrolases --- Zinc Compounds --- Metals, Heavy --- Boron Compounds --- Enzymes --- Transition Elements --- Inorganic Chemicals --- Organic Chemicals --- Chemicals and Drugs --- Elements --- Metals --- Enzymes and Coenzymes --- Animal Biochemistry --- Human Anatomy & Physiology --- Health & Biological Sciences --- Inorganic chemistry. --- Biochemistry. --- Molecular biology. --- Cell biology. --- Biophysics. --- Biological physics. --- Inorganic Chemistry. --- Biochemistry, general. --- Molecular Medicine. --- Cell Biology. --- Biological and Medical Physics, Biophysics. --- Biological physics --- Biology --- Medical sciences --- Physics --- Cell biology --- Cellular biology --- Cells --- Molecular biochemistry --- Molecular biophysics --- Biochemistry --- Biophysics --- Biomolecules --- Systems biology --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Chemistry --- Inorganic chemistry --- Inorganic compounds --- Composition
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