Literature DB >> 9786710

Determination of protein-protein interactions by matrix-assisted laser desorption/ionization mass spectrometry.

T B Farmer1, R M Caprioli.   

Abstract

A number of different procedures have been developed for use with matrix-assisted laser desorption/ionization mass spectrometry (MALDI/MS) for the analysis of non-covalent protein-protein complexes. These include use of specific matrix and laser combinations, accumulation of "first shot" spectra, modification of pH and solvent conditions during sample preparation and use of cross-linking agents to attach the monomers covalently to each other in the complex. The results have shown the techniques to be effective with some but not all complexes, although cross-linking is the most successful. The physical and chemical nature of the complex is critical and therefore a diversity of approaches is recommended for such studies.

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Year:  1998        PMID: 9786710     DOI: 10.1002/(SICI)1096-9888(199808)33:8<697::AID-JMS711>3.0.CO;2-H

Source DB:  PubMed          Journal:  J Mass Spectrom        ISSN: 1076-5174            Impact factor:   1.982


  34 in total

1.  Preservation and detection of specific antibody--peptide complexes by matrix-assisted laser desorption ionization mass spectrometry.

Authors:  J G Kiselar; K M Downard
Journal:  J Am Soc Mass Spectrom       Date:  2000-08       Impact factor: 3.109

2.  A study of peptide-peptide interactions using MALDI ion mobility o-TOF and ESI mass spectrometry.

Authors:  Amina S Woods; John M Koomen; Brandon T Ruotolo; Kent J Gillig; David H Russel; Katrin Fuhrer; Marc Gonin; Thomas F Egan; J Albert Schultz
Journal:  J Am Soc Mass Spectrom       Date:  2002-02       Impact factor: 3.109

3.  Formation and fate of ion pairs during MALDI analysis: anion adduct generation as an indicative tool to determine ionization processes.

Authors:  Ralf Krüger; Michael Karas
Journal:  J Am Soc Mass Spectrom       Date:  2002-10       Impact factor: 3.109

4.  Detection of specific noncovalent interaction of peptide with DNA by MALDI-TOF.

Authors:  Shi-Zhong Luo; Yan-Mei Li; Wei Qiang; Yu-Fen Zhao; Hiroshi Abe; Tadashi Nemoto; Xu-Rong Qin; Hiroshi Nakanishi
Journal:  J Am Soc Mass Spectrom       Date:  2004-01       Impact factor: 3.109

5.  Mass spectrometric determination of association constants of adenylate kinase with two noncovalent inhibitors.

Authors:  Jürg M Daniel; Gregor McCombie; Silke Wendt; Renato Zenobi
Journal:  J Am Soc Mass Spectrom       Date:  2003-05       Impact factor: 3.109

6.  Compelling advantages of negative ion mode detection in high-mass MALDI-MS for homomeric protein complexes.

Authors:  Stefanie Mädler; Konstantin Barylyuk; Elisabetta Boeri Erba; Robert J Nieckarz; Renato Zenobi
Journal:  J Am Soc Mass Spectrom       Date:  2011-12-01       Impact factor: 3.109

7.  Does chemical cross-linking with NHS esters reflect the chemical equilibrium of protein-protein noncovalent interactions in solution?

Authors:  Stefanie Mädler; Markus Seitz; John Robinson; Renato Zenobi
Journal:  J Am Soc Mass Spectrom       Date:  2010-07-07       Impact factor: 3.109

8.  How far can we go with structural mass spectrometry of protein complexes?

Authors:  Michal Sharon
Journal:  J Am Soc Mass Spectrom       Date:  2010-01-04       Impact factor: 3.109

9.  Molecular cloning, expression, and cytokinin (6-benzylaminopurine) antagonist activity of peanut (Arachis hypogaea) lectin SL-I.

Authors:  Monika Pathak; Bharat Singh; Amit Sharma; Praveen Agrawal; Santosh B Pasha; Hasi R Das; Rakha H Das
Journal:  Plant Mol Biol       Date:  2006-08-29       Impact factor: 4.076

10.  Intracellular protein interaction mapping with FRET hybrids.

Authors:  Xia You; Annalee W Nguyen; Abeer Jabaiah; Mark A Sheff; Kurt S Thorn; Patrick S Daugherty
Journal:  Proc Natl Acad Sci U S A       Date:  2006-11-27       Impact factor: 11.205

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