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Sinopsis
The number of protein isoforms in proteomes can be two to three orders of magnitude higher than the number of genes in the genomes. This is in large part due to posttranslational modifications of proteins that provide covalent alterations to protein backbones and side chains that increase proteome complexities. Greater than 5% of the genes in the human genome encode enzymes that perform such modifications, including hundreds of protein kinases and opposing phosphatases, ubiquitinyl ligases, acetylases and deacetylases, methyl transferases and glycosyl transferases. The major classes of posttranslational modifications (PTM) are codified according to types of residues modified, underlying chemistry, PTM catalysts and biological consequences.
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Professor Walsh is currently the Hamilton Kuhn Professor of Biological Chemistry and Molecular Pharmacology at Harvard Medical School. He is one of the leading enzymologists in the world. He has published over 600 scientific articles and his book, Enzymatic Reaction Mechanisms (WH Freeman), has educated generations of enzymologists.
De la contraportada
More than five percent of the genes in higher eukaryotic genomes encode enzymes that posttranslationally modify proteins, greatly expanding the complexity and diversity of proteomes. This book examines the molecular logic of the major types of covalent modifications of proteins and their biological consequences.
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Posttranslational Modification of Proteins: Expanding Nature's Inventory
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Roberts and Company Publishers, 2005
ISBN 10: 0974707732
ISBN 13: 9780974707730
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Posttranslational Modification of Proteins: Expanding Natures Inventory
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Roberts and Company Publishers, 2005
ISBN 10: 0974707732
ISBN 13: 9780974707730
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Posttranslational Modification of Proteins: Expanding Nature*s Inventory
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Roberts and Company Publishers, 2005
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ISBN 13: 9780974707730
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Posttranslational Modification of Proteins: Expanding Nature's Inventory
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Roberts and Company Publishers, 2005
ISBN 10: 0974707732
ISBN 13: 9780974707730
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