Literature DB >> 28345863

Native Mass Spectrometry of Recombinant Proteins from Crude Cell Lysates.

Jinrui Gan1, Gili Ben-Nissan1, Galina Arkind1, Mark Tarnavsky1, Devin Trudeau1, Lianet Noda Garcia1, Dan S Tawfik1, Michal Sharon1.   

Abstract

Determining the properties of proteins prior to purification saves time and labor. Here, we demonstrate a native mass spectrometry approach for rapid characterization of overexpressed proteins directly in crude cell lysates. The method provides immediate information on the identity, solubility, oligomeric state, overall structure, and stability, as well as ligand binding, without the need for purification.

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Year:  2017        PMID： 28345863      PMCID： PMC5702260          DOI： 10.1021/acs.analchem.7b00398

Source DB:  PubMed          Journal:  Anal Chem        ISSN： 0003-2700            Impact factor:   6.986


  24 in total

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  17 in total

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2.  Surface-Induced Dissociation: An Effective Method for Characterization of Protein Quaternary Structure.

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3.  Surface-Induced Dissociation for Protein Complex Characterization.

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Journal:  Methods Mol Biol       Date:  2022

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Review 5.  The application of ion-mobility mass spectrometry for structure/function investigation of protein complexes.

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Review 7.  Approaches to Heterogeneity in Native Mass Spectrometry.

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8.  Thermal Analysis of a Mixture of Ribosomal Proteins by vT-ESI-MS: Toward a Parallel Approach for Characterizing the Stabilitome.

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9.  Analysis of Tagged Proteins Using Tandem Affinity-Buffer Exchange Chromatography Online with Native Mass Spectrometry.

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