Protein mass spectrometry tools

After incubation the protein-compound complex is directly infused into a Bruker Daltonics. The protein—compound complex is sprayed in 10 mM ammonium acetate, pH 6. Any sites of biotinylation in the complex that are lost indicate a binding surface. National Center for Biotechnology Information , U. Methods Mol Biol. Author manuscript; available in PMC Nov 9.

Jared R. Auclair , Mohan Somasundaran , Karin M. Green , James E. Evans , Celia A. Schiffer , Dagmar Ringe , Gregory A. Petsko , and Jeffrey N. Copyright and License information Disclaimer. Copyright notice. The publisher's final edited version of this article is available at Methods Mol Biol. Abstract The small quantities of protein required for mass spectrometry MS make it a powerful tool to detect binding protein—protein, protein—small molecule, etc.

Introduction Intrinsically disordered regions and proteins by their disordered nature make it inherently difficult to crystallize and thus determine their three dimensional structures as well as identifying intermolecular interactions 1. Omix C18 Tip Agilent. Mass Spectrometry and Data Analysis Any mass spectrometer. Data Analysis Flex Analysis Bruker. Data Analysis Bruker. Methods Be sure to dispose of all hazardous chemicals appropriately.

Open in a separate window. Identify peptides and cross-linked peptides using the following criteria: Trypsin-specific cleavages are present arginine or lysine. Intermolecular cross-links are seen in only Protein A and B cross-linked samples. Footnotes 1 Cross-linking: multiple cross-linkers with different spacer arms can be used to give an idea of the distance at which one residue is from another.

References 1. Dunker AK, et al. Intrinsically disordered protein. Translated from eng. J Mol Graph Model. Proteomics by mass spectrometry: approaches, advances, and applications. Annu Rev Biomed Eng. Chemical cross-linking and mass spectrometry for protein structural modeling. J Mol Biol. Methods to study protein dynamics and folding by mass spectrometry. J Mass Spectrom. Anal Chem. Mapping the topology and determination of a low-resolution three-dimensional structure of the calmodulin-melittin complex by chemical cross-linking and high-resolution FTICRMS: direct demonstration of multiple binding modes.

Sinz A. Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes. Trester-Zedlitz M, et al. A modular cross-linking approach for exploring protein interactions.

J Am Chem Soc. Chemical cross-linking and mass spectrometry to map three-dimensional protein structures and protein-protein interactions. Mass Spectrom Rev. Auclair JR, et al. Mass spectrometry analysis of HIV-1 Vif reveals an increase in ordered structure upon oligomerization in regions necessary for viral infectivity.

Leitner A, et al. Probing native protein structures by chemical cross-linking, mass spec-trometry, and bioinformatics. Mol Cell Proteomics. Pandey A, Mann M. Proteomics to study genes and genomes.

Gavin AC, et al. Functional organization of the yeast proteome by systematic analysis of protein complexes. Ho Y, et al. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Blagoev B, et al. A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling.

Nat Biotechnol. Back JW, et al. Identification of cross-linked peptides for protein interaction studies using mass spectrometry and 18O labeling. Proteolytic 18O labeling for comparative proteomics: model studies with two serotypes of adenovirus. Strategies for stabilizing super-oxide dismutase SOD1 , the protein destabilized in the most common form of familial amyotrophic lateral sclerosis.

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Jump to main content. Jump to site search. You do not have JavaScript enabled. Please enable JavaScript to access the full features of the site or access our non-JavaScript page. Issue 11, From the journal: Chemical Society Reviews. Mass spectrometry based tools to investigate protein—ligand interactions for drug discovery.

Kamila J. Pacholarz , a Rachel A. Garlish , b Richard J. Taylor b and Perdita E. You have access to this article. Please wait while we load your content Something went wrong.

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