Protein acetylation : methods and protocols /

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Bibliographic Details
Imprint:New York : Humana Press : Springer, ©2013.
Description:1 online resource (xi, 266 pages) : illustrations (some color)
Language:English
Series:Methods in molecular biology, 1940-6029 ; 981
Methods in molecular biology (Clifton, N.J.) ; v. 981.
Subject:
Format: E-Resource Book
URL for this record:http://pi.lib.uchicago.edu/1001/cat/bib/11173645
Hidden Bibliographic Details
Other authors / contributors:Hake, Sandra B.
Janzen, Christian J.
ISBN:9781627033053
162703305X
1627033041
9781627033046
9781627033046
Digital file characteristics:text file PDF
Notes:Includes bibliographical references and index.
English.
Print version record.
Summary:Thousands of proteins have been identified to be acetylated. Immense research power has been dedicated to experiments to solve the biological implications of each and every protein acetylation. Two particular sites of protein acetylation have been described intensively: the N-terminal methionine residue of a nascent protein and lysine residues within a protein. In Protein Acetylation: Methods and Protocols, expert researchers in the field detail many of the methods which are now commonly used to study protein acetylation. These include methods and techniques for identification of protein acetylation, column- and gel electrophoresis-based approaches, computationally prediction, and the biological response to protein acetylation. 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, Protein Acetylation: Methods and Protocols seeks to aid scientists in the further study of the technical aspects involved in understanding protein acetylation.
Other form:Print version: Protein acetylation. New York : Humana Press ; Springer, ©2013 1627033041
Standard no.:10.1007/978-1-62703-305-3

MARC

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505 0 0 |t Validation of protein acetylation by mass spectrometry /  |r Barry M. Zee and Benjamin A. Garcia --  |t Application of the CIRAD mass spectrometry approach for lysine acetylation site discovery /  |r Caroline A. Evans [and others] --  |t Application of the MIDAS approach for analysis of lysine acetylation sites /  |r Caroline A. Evans [and others] --  |t Application of high content biology to yield quantitative spatial proteomic information on protein acetylations /  |r Bernard M. Corfe [and others] --  |t Towards the N-Terminal acetylome : an N-Terminal acetylated peptide enrichment method using CNBr-activated sepharose resin /  |r Xumin Zhang and Peter Højrup --  |t Identification and analysis of o-acetylated sialoglycoproteins /  |r Chandan Mandal and Chitra Mandal --  |t HPLC-based quantification of in vitro N-terminal acetylation /  |r Rune H. Evjenth [and others] --  |t Separation and purification of multiply acetylated proteins using cation-exchange chromatography /  |r Romeo Papazyan and Sean D. Taverna --  |t In-gel N-acetylation for the quantification of the degree of protein in vivo N-terminal acetylation /  |r Petra Van Damme [and others] --  |t Computational prediction of lysine acetylation proteome-wide /  |r Amrita Basu --  |t Generation and characterization of pan-specific anti-acetyllysine antibody /  |r Wei Xu and Shimin Zhao --  |t Using functional proteome microarrays to study protein lysine acetylation /  |r Jin-ying Lu [and others] --  |t Quantitation of nucleosome acetylation and other histone posttranslational modifications using microscale NU-ELISA /  |r Bo Dai, Charles Giardina, and Theodore P. Rasmussen --  |t Preparing semisynthetic and fully synthetic histones H3 and H4 to modify the nucleosome core /  |r John C. Shimko [and others] --  |t Production of amino-terminally acetylated recombinant proteins in E. coli /  |r Matthew Johnson, Michael A. Geeves, and Daniel P. Mulvihill --  |t Identification of lysine acetyltransferase substrates using bioorthogonal chemical proteomics /  |r Markus Grammel and Howard C. Hang --  |t Nonradioactive in vitro assays for histone deacetylases /  |r Alexander-Thomas Hauser, Julia M. Gajer (nee Wagner), and Manfred Jung --  |t Fluorescence-based acetylation assay using thiol-sensitive probes /  |r Tielong Gao, Chao Yang, and Yujun George Zheng --  |t Analysis of protein acetyltransferase structure-function relation by surface-enhanced raman scattering (SERS): a tool to screen and characterize small molecule modulators /  |r Mohammed Arif [and others]. 
504 |a Includes bibliographical references and index. 
588 0 |a Print version record. 
520 |a Thousands of proteins have been identified to be acetylated. Immense research power has been dedicated to experiments to solve the biological implications of each and every protein acetylation. Two particular sites of protein acetylation have been described intensively: the N-terminal methionine residue of a nascent protein and lysine residues within a protein. In Protein Acetylation: Methods and Protocols, expert researchers in the field detail many of the methods which are now commonly used to study protein acetylation. These include methods and techniques for identification of protein acetylation, column- and gel electrophoresis-based approaches, computationally prediction, and the biological response to protein acetylation. 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, Protein Acetylation: Methods and Protocols seeks to aid scientists in the further study of the technical aspects involved in understanding protein acetylation. 
546 |a English. 
650 0 |a Acetylation  |v Laboratory manuals. 
650 0 |a Proteins  |v Laboratory manuals. 
650 0 |a Acetylation.  |0 http://id.loc.gov/authorities/subjects/sh87001826 
650 0 |a Proteins.  |0 http://id.loc.gov/authorities/subjects/sh85107666 
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650 6 |a Acétylation  |v Manuels de laboratoire. 
650 6 |a Protéines  |v Manuels de laboratoire. 
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650 7 |a Acetylation  |2 fast 
650 7 |a Proteins  |2 fast 
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653 0 0 |a proteins 
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653 1 0 |a Proteins and Enzymes 
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830 0 |a Methods in molecular biology (Clifton, N.J.) ;  |v v. 981.  |x 1064-3745 
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