The majority of all proteins undergo posttranslational modifications that significantly alter their physical and chemical properties, including their folding and conformation distribution, their stability, and, consequently, their activity and function. In Posttranslational Modifications of Proteins: Tools for Functional Proteomics, Christoph Kannicht and a panel of highly experienced researchers describe readily reproducible methods for detecting and analyzing the most important of these modifications, particularly with regard to protein function, proteome research, and the characterization of pharmaceutical proteins. Among the methods presented are those for analyzing the assignment of disulfide bond sites in proteins, protein N-glycosylation and protein O-glycosylation, and oligosaccharides present at specific single glycosylation sites in a protein. Additional powerful techniques facilitate the analysis of glycosylphosphatidylinositols, lipid modifications, protein phosphorylation and sulfation, protein methylation and acetylation, a-amidation, g-glutamate, isoaspartate, and lysine hydroxylation.
Comprehensive and state-of-the-art, Posttranslational Modifications of Proteins: Tools for Functional Proteomics serves as a highly practical guide for all investigators of protein structure-function relationships not only in chemical and pharmaceutical research, but also throughout the rapidly growing field of functional proteomics.
Die Inhaltsangabe kann sich auf eine andere Ausgabe dieses Titels beziehen.
The majority of all proteins undergo posttranslational modifications that significantly alter their physical and chemical properties, including their folding and conformation distribution, their stability, and, consequently, their activity and function. In Posttranslational Modifications of Proteins: Tools for Functional Proteomics, Christoph Kannicht and a panel of highly experienced researchers describe readily reproducible methods for detecting and analyzing the most important of these modifications, particularly with regard to protein function, proteome research, and the characterization of pharmaceutical proteins. Among the methods presented are those for analyzing the assignment of disulfide bond sites in proteins, protein N-glycosylation and protein O-glycosylation, and oligosaccharides present at specific single glycosylation sites in a protein. Additional powerful techniques facilitate the analysis of glycosylphosphatidylinositols, lipid modifications, protein phosphorylation and sulfation, protein methylation and acetylation, a-amidation, g-glutamate, isoaspartate, and lysine hydroxylation.
Comprehensive and state-of-the-art, Posttranslational Modifications of Proteins: Tools for Functional Proteomics serves as a highly practical guide for all investigators of protein structure-function relationships not only in chemical and pharmaceutical research, but also throughout the rapidly growing field of functional proteomics.
„Über diesen Titel“ kann sich auf eine andere Ausgabe dieses Titels beziehen.
Anbieter: Books From California, Simi Valley, CA, USA
hardcover. Zustand: Good. Ex- library copy with stamps and stickers. Artikel-Nr. mon0003287952
Anzahl: 1 verfügbar
Anbieter: Anybook.com, Lincoln, Vereinigtes Königreich
Zustand: Poor. This is an ex-library book and may have the usual library/used-book markings inside.This book has hardback covers. In poor condition, suitable as a reading copy. Please note the Image in this listing is a stock photo and may not match the covers of the actual item,750grams, ISBN:9780896036789. Artikel-Nr. 9230529
Anzahl: 1 verfügbar
Anbieter: Ria Christie Collections, Uxbridge, Vereinigtes Königreich
Zustand: New. In English. Artikel-Nr. ria9780896036789_new
Anzahl: Mehr als 20 verfügbar
Anbieter: Kennys Bookstore, Olney, MD, USA
Zustand: New. Describes reproducible methods for detecting and analyzing the posttranslational modifications of protein, particularly with regard to protein function, proteome research, and the characterization of pharmaceutical proteins. This work also presents methods for analyzing the assignment of disulfide bond sites in proteins. Editor(s): Kannicht, Christoph. Series: Methods in Molecular Biology. Num Pages: 322 pages, 19 black & white illustrations, biography. BIC Classification: PSD. Category: (P) Professional & Vocational; (UP) Postgraduate, Research & Scholarly; (UU) Undergraduate. Dimension: 234 x 156 x 19. Weight in Grams: 660. . 2002. Hardback. . . . . Books ship from the US and Ireland. Artikel-Nr. V9780896036789
Anzahl: 15 verfügbar
Anbieter: AHA-BUCH GmbH, Einbeck, Deutschland
Buch. Zustand: Neu. Neuware - The majority of all proteins undergo posttranslational modifications that significantly alter their physical and chemical properties, including their folding and conformation distribution, their stability, and, consequently, their activity and function. In Posttranslational Modifications of Proteins: Tools for Functional Proteomics, Christoph Kannicht and a panel of highly experienced researchers describe readily reproducible methods for detecting and analyzing the most important of these modifications, particularly with regard to protein function, proteome research, and the characterization of pharmaceutical proteins. Among the methods presented are those for analyzing the assignment of disulfide bond sites in proteins, protein N-glycosylation and protein O-glycosylation, and oligosaccharides present at specific single glycosylation sites in a protein. Additional powerful techniques facilitate the analysis of glycosylphosphatidylinositols, lipid modifications, protein phosphorylation and sulfation, protein methylation and acetylation, a-amidation, g-glutamate, isoaspartate, and lysine hydroxylation. Comprehensive and state-of-the-art, Posttranslational Modifications of Proteins: Tools for Functional Proteomics serves as a highly practical guide for all investigators of protein structure-function relationships not only in chemical and pharmaceutical research, but also throughout the rapidly growing field of functional proteomics. Artikel-Nr. 9780896036789
Anzahl: 2 verfügbar