Chemical proteomics : methods and protocols / edited by Gerard Drewes and Marcus Bantscheff.
Contributor(s): Drewes, Gerard | Bantscheff, MarcusMaterial type: TextSeries: Methods in molecular biology (Clifton, N.J.): v. 803.Publisher: New York : Humana Press, ©2012Description: 1 online resource (xi, 313 pages)Content type: text Media type: computer Carrier type: online resourceISBN: 9781617793646; 1617793647; 1617793639; 9781617793639Subject(s): Proteomics -- Laboratory manuals | Biochemistry -- Laboratory manuals | Investigative Techniques | Biological Science Disciplines | Genomics | Publication Formats | Chemical Phenomena | Chemistry | Analytical, Diagnostic and Therapeutic Techniques and Equipment | Natural Science Disciplines | Publication Characteristics | Computational Biology | Genetics | Phenomena and Processes | Disciplines and Occupations | Biology | Biochemistry | Methods | Proteomics | Laboratory Manuals | Chemistry Techniques, Analytical | Biochemical Phenomena | Biochemistry | Proteomics | Life sciences | Proteomics | Biochemistry | Protein Science | eiwitten | proteins | eiwitexpressieanalyse | levenswetenschappenGenre/Form: Electronic books. | Laboratory manuals. Additional physical formats: Printed edition:: No titleDDC classification: 572/.6 LOC classification: QP551 | .C44 2012Online resources: Click here to access online
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Mass spectrometry-based chemoproteomic approaches -- Chemical proteomics in drug discovery -- Compound immobilization and drug-affinity chromatography -- Affinity-based chemoproteomics with small molecule-peptide conjugates -- A chemical proteomic probe for detecting dehydrogenases: Catechol rhodanine -- Probing proteomes with benzophenone photoprobes -- Biotinylated probes for the analysis of protein modification by electrophiles -- Profiling of methyltransferases and other S-adenosyl-l: -homocysteine-binding proteins by capture compound mass spectrometry -- Identifying cellular targets of small-molecule probes and drugs with biochemical enrichment and SILAC -- Determination of kinase inhibitor potencies in cell extracts by competition binding assays and isobaric mass tags -- Affinity-based profiling of dehydrogenase subproteomes -- Probing the specificity of protein-protein interactions by quantitative chemical proteomics -- Fluorescence-based proteasome activity profiling -- Chemical cross-linking and high-resolution mass spectrometry to study protein-drug interactions -- Monitoring ligand modulation of protein-protein interactions by chemical cross-linking and high-mass MALDI mass spectrometry -- Time-controlled transcardiac perfusion crosslinking for in vivo interactome studies -- Ligand discovery using small-molecule microarrays -- Working with small molecules: Preparing and storing stock solutions and determination of kinetic solubility -- A database for chemical proteomics: ChEBI -- Working with small molecules: Rules-of-thumb of "Drug likeness."
Online resource; title from PDF title page (SpringerProtocols, viewed Nov. 30, 2011).
The multidisciplinary science of chemical proteomics studies how small molecules of synthetic or natural origin bind to proteins and modulate their function. In Chemical Proteomics: Methods and Protocols, expert researchers in the field provide key techniques to investigate chemical proteomics focusing on analytical strategies, how probes are generated, techniques for the discovery of small molecule targets and the probing of target function, and small molecule ligand and drug discovery. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and key tips on troubleshooting and avoiding known pitfalls. Authoritative and practical, Chemical Proteomics : Methods and Protocols seeks to provide methodologies that will contribute to a wider application of chemical proteomics methods in biochemical and cell biological laboratories.
Includes bibliographical references and index.