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008 100301s2002 xxu| s |||| 0|eng d
020 _a9781592591817
_9978-1-59259-181-7
024 7 _a10.1385/1592591817
_2doi
050 4 _aQH573-671
072 7 _aPSF
_2bicssc
072 7 _aSCI017000
_2bisacsh
072 7 _aPSF
_2thema
082 0 4 _a571.6
_223
245 1 0 _aPosttranslational Modification of Proteins
_h[electronic resource] :
_bTools for Functional Proteomics /
_cedited by Christoph Kannicht.
250 _a1st ed. 2002.
264 1 _aTotowa, NJ :
_bHumana Press :
_bImprint: Humana,
_c2002.
300 _aXI, 322 p. 19 illus.
_bonline resource.
336 _atext
_btxt
_2rdacontent
337 _acomputer
_bc
_2rdamedia
338 _aonline resource
_bcr
_2rdacarrier
347 _atext file
_bPDF
_2rda
490 1 _aMethods in Molecular Biology,
_x1940-6029 ;
_v194
505 0 _aAssignment of Disulfide Bonds in Proteins by Chemical Cleavage and Peptide Mapping by Mass Spectrometry -- Carbohydrate Composition Analysis of Glycoproteins Using Highly Sensitive Fluorescence Detection Methods -- Enzymatical Hydrolysis of N-Glycans from Glycoproteins and Fluorescent Labeling by 2-Aminobenzamide (2-AB) -- Separation of N-Glycans by HPLC -- Enzymatic Sequence Analysis of N-Glycans -- Immunological Detection of O-GlcNAc -- Analysis of O-Glycosylation -- Characterization of Site-Specific Glycosylation -- Monitoring Glycosylation of Therapeutic Glycoproteins for Consistency Using Highly Fluorescent Anthranilic Acid -- Metabolic Labeling and Structural Analysis of Glycosylphosphatidylinositols from Parasitic Protozoa -- Analysis of S-Acylation of Proteins -- Immunoblotting Methods for the Study of Protein Ubiquitination -- Analysis of Methylation and Acetylation in E. coli Ribosomal Proteins -- Identification of In Vivo Protein Phosphorylation Sites with Mass Spectrometry -- Analysis of Tyrosine-O-Sulfation -- ?-Amidated Peptides: Approaches for Analysis -- ?-Glutamate and p-Hydroxyaspartate in Proteins -- Detection of isoAspartate Residues as a Posttranslational Modification of Proteins and Peptides -- Lysine Hydroxylation and Crosslinking of Collagen -- Heterologous Expression in Endocrine Cells for Analysis of Posttranslational Modifications -- 2D-Electrophoresis: Detection of Glycosylation and Influence on Spot Pattern.
520 _aThe 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.
650 0 _aCytology.
650 1 4 _aCell Biology.
700 1 _aKannicht, Christoph.
_eeditor.
_4edt
_4http://id.loc.gov/vocabulary/relators/edt
710 2 _aSpringerLink (Online service)
773 0 _tSpringer Nature eBook
776 0 8 _iPrinted edition:
_z9780896036789
776 0 8 _iPrinted edition:
_z9781489938633
776 0 8 _iPrinted edition:
_z9781489938640
830 0 _aMethods in Molecular Biology,
_x1940-6029 ;
_v194
856 4 0 _uhttps://doi.org/10.1385/1592591817
912 _aZDB-2-PRO
999 _c7944
_d7944