Posttranslational Modifications of Proteins

Автор(ы):Kannicht C.
Год изд.:2002
Описание: 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 coverthe 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, activity, and, consequently, function ofthe proteins. Moreover, the modification itself can act as an added functional group. 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.
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1 Assignment of Bisulfide Bonds in Proteins by Chemical Cleavage and Peptide Mapping by Mass Spectrometry
  Jiang Wu and J. ThrockWatson [1]
2 Carbohydrate Composition Analysis of Glycoproteins Using Highly Sensitive Fluorescence Detection Methods
  George N. Saddle, Mary Beth Ebert, Shirish T. Dhume, and Kalyan R. Anumula [23]
3 Enzymatical Hydrolysis of N-Glycans from Glycoproteins and Fluorescent Labeling by 2-Aminobenzamide (2-AB)
  Rolf Nuck [37]
4 Separation of N-Glycans by HPLC
  Martin Gohlke [45]
5 Enzymatic Sequence Analysis of N-Glycans
  Christoph Kannicht and Anke Flechner [63]
6 Immunological Detection of O-GlcNAc
  Monika Rex-Mathes, Jurgen Koch, Sabine Werner, Lee S. Griffith, and Brigitte Schmitz [73]
7 Analysis of O-Glycosylation
  Juan J. Calvete and Libia Sanz [89]
8 Characterization of Site-Specific Glycosylation
  Katalin F. Medzihradszky [101]
9 Monitoring Glycosylation of Therapeutic Glycoproteins for Consistency Using Highly Fluorescent Anthranilic Acid
  Shirish T. Dhume, Mary Beth Ebert, George N. Saddle, and Kalyan R. Anumula [127]
10 Metabolic Labeling and Structural Analysis of Glycosylphosphatidylinositols from Parasitic Protozoa
  Peter Gerold and Ralph T. Schwarz [143]
11 Analysis of S-Acylation of Proteins
  Michael Veit, Evgeni Ponimaskin, and Michael F. G. Schmidt [159]
12 Immunoblotting Methods for the Study of Protein Ubiquitination
  Edward G. Mimnaugh and Leonard M. Neckers [179]
13 Analysis of Methylation and Acetylation in E. coll Ribosomal Proteins
  Randy J. Arnold and James P. Reilly [205]
14 Identification of In Vivo Protein Phosphorylation Sites with Mass Spectrometry
  Jun Qin and Xiaolong Zhang [211]
15 Analysis of Tyrosine-O-Sulfation
  Jens R. Bundgaard, Anders H. Johnsen, and Jens F. Rehfeld [223]
16 (?)-Amidated Peptides: Approaches for Analysis
  Gregory P. Mueller and William J. Driscoll [241]
17 (?)-Glutamate and (?)-Hydroxyaspartate in Proteins
  Francis J. Castellino, Victoria A. Ploplis, and Li Zhang [259]
18 Detection of isoAspartate Residues as a Posttranslational Modification of Proteins and Peptides
  Verne Schirch, Sonia Delle Fratte, and Marti no di Salvo [269]
19 Lysine Hydroxylation and Crosslinking of Collagen
  Mitsuo Yamauchi and Masashi Shiiba [277]
20 Heterologous Expression in Endocrine Cells for Analysis of Posttranslational Modifications
  Jens R. Bundgaard [291]
21 2D-Electrophoresis: Detection of Glycosylation and Influence on Spot Pattern
  Klemens Loster and Christoph Kannicht [301]
Index [317]
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