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Posttranslational Modification of Proteins: Tools for Functional Proteomics

ISBN-13: 9780896036789 / Angielski / Twarda / 2002 / 322 str.

Christoph Kannicht; Christoph Kannicht
Posttranslational Modification of Proteins: Tools for Functional Proteomics Kannicht, Christoph 9780896036789 Humana Press - książkaWidoczna okładka, to zdjęcie poglądowe, a rzeczywista szata graficzna może różnić się od prezentowanej.

Posttranslational Modification of Proteins: Tools for Functional Proteomics

ISBN-13: 9780896036789 / Angielski / Twarda / 2002 / 322 str.

Christoph Kannicht; Christoph Kannicht
cena 403,47 zł
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Posttranslational Modifications of Proteins: Tools for Functional Proteomics is a compilation of detailed protocols needed to detect and analyze the most important co- and posttranslational modifications of proteins. Though, for reasons of simplicity not explicitly mentioned in the title, both kinds of modifications are covered, whether they occur during, or after, biosynthesis of the protein. My intention was to cover the most significant protein modifications, focusing on the fields of protein function, proteome research, and the characterization of pharmaceutical proteins. The majority of all proteins undergo co- and/or posttranslational modifications. Knowledge of these modifications is extremely important, since they may alter physical and chemical properties, folding, conformation distribution, stability, act- ity, and, consequently, function of the proteins. Moreover, the modification itself can act as an added functional group. Examples of the biological effects of protein mo- fications include: phosphorylation for signal transduction, ubiquitination for p- teolysis, attachment of fatty acids for membrane anchoring or association, glycosylation for protein half-life, targeting, cell-cell and cell-matrix interactions, and carboxylation in protein-ligand binding to name just a few. Full understanding of a specific protein structure-function relationship requires detailed information not only on its amino acid sequence, which is determined by the corresponding DNA sequence, but also on the presence and structure of protein modifications.

Kategorie:
Nauka, Biologia i przyroda
Kategorie BISAC:
Religion > Judaism - Kabbalah & Mysticism
Self-Help > General
Body, Mind & Spirit > General
Wydawca:
Humana Press
Seria wydawnicza:
Methods in Molecular Biology (Cloth)
Język:
Angielski
ISBN-13:
9780896036789
Rok wydania:
2002
Wydanie:
2002
Numer serii:
000014950
Ilość stron:
322
Waga:
0.66 kg
Wymiary:
23.5 x 15.5
Oprawa:
Twarda
Wolumenów:
01
Dodatkowe informacje:
Bibliografia
Wydanie ilustrowane

"As indicated by the editor, this book will be useful to researchers involved in elucidating protein structure and function as well as those working to design proteins with specific function...this book offers detailed analytical protocols for identifying and characterizing most types of co- and post- translational modifications" - Pharmaceutical Research

"This book provides researchers in the biological sciences with the most updated methods to investigate co- and/or post-translational modifications of proteins...Either trained professionals and students working in the field of proteomics can take benefit for their research." - Proteomics

"It will definitely find appreciative readers among a wide audience of glycobiologists, biochemists, molecular biologists, biotechnologists, and researchers specializing in pharmacology and molecular medicine. This book will be a very useful tool for teachers and students of universities and institutes." -Biochemistry

Assignment of Disulfide Bonds in Proteins by Chemical Cleavage and Peptide Mapping by Mass Spectrometry Jiang Wu and J. Throck Watson Carbohydrate Composition Analysis of Glycoproteins Using Highly Sensitive Fluorescence Detection Methods George N. Saddic, Mary Beth Ebert, Shirish T. Dhume, and Kalyan R. Anumula Enzymatical Hydrolysis of N-Glycans from Glycoproteins and Fluorescent Labeling by 2-Aminobenzamide (2-AB) Rolf Nuck Separation of N-Glycans by HPLC, Martin Gohlke. Enzymatic Sequence Analysis of N-Glycans Christoph Kannicht and Anke Flechner Immunological Detection of O-GlcNAc Monika Rex-Mathes, Jürgen Koch, Sabine Werner, Lee S. Griffith, and Brigitte Schmitz Analysis of O-Glycosylation Juan J. Calvete and Libia Sanz Characterization of Site-Specific Glycosylation Katalin F. Medzihradszky Monitoring Glycosylation of Therapeutic Glycoproteins for Consistency Using Highly Fluorescent Anthranilic Acid Shirish T. Dhume, Mary Beth Ebert, George N. Saddic, and Kalyan R. Anumula Metabolic Labeling and Structural Analysis of Glycosylphosphatidylinositols from Parasitic Protozoa Peter Gerold and Ralph T. Schwarz Analysis of S-Acylation of Proteins Michael Veit, Evgeni Ponimaskin, and Michael F. G. Schmidt Immunoblotting Methods for the Study of Protein Ubiquitination Edward G. Mimnaugh and Leonard M. Neckers Analysis of Methylation and Acetylation in E. coli Ribosomal Proteins Randy J. Arnold and James P. Reilly Identification of In Vivo Protein Phosphorylation Sites with Mass Spectrometry Jun Qin and Xiaolong Zhang Analysis of Tyrosine-O-Sulfation Jens R. Bundgaard, Anders H. Johnsen, and Jens F. Rehfeld a-Amidated Peptides: Approaches for Analysis Gregory P. Mueller and William J. Driscoll g-Glutamate and b-Hydroxyaspartate inProteins Francis J. Castellino, Victoria A. Ploplis, and Li Zhang Detection of isoAspartate Residues as a Posttranslational Modification of Proteins and Peptides Verne Schirch, Sonia Delle Fratte, and Martino di Salvo Lysine Hydroxylation and Crosslinking of Collagen Mitsuo Yamauchi and Masashi Shiiba Heterologous Expression in Endocrine Cells for Analysis of Posttranslational Modifications Jens R. Bundgaard 2D-Electrophoresis: Detection of Glycosylation and Influence on Spot Pattern Klemens Löster and Christoph Kannicht

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.



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