ArticleProtein science : a publication of the Protein Society1997
Surface topology of Minibody by selective chemical modifications and mass spectrometry.
Article in Protein science : a publication of the Protein Society, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed.
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- Protein design: toward functional metalloenzymes.Chemical reviews · 2014Review
- Mapping protein surface accessibility via an electron transfer dissociation selectively cleavable hydrazone probe.Molecular & cellular proteomics : MCP · 2012Article
- Apolipoprotein A-II-mediated conformational changes of apolipoprotein A-I in discoidal high density lipoproteins.The Journal of biological chemistry · 2012Article
- Structural characterization of the conformational change in calbindin-D28k upon calcium binding using differential surface modification analyzed by mass spectrometry.Biochemistry · 2009Article
- Using metal-catalyzed oxidation reactions and mass spectrometry to identify amino acid residues within 10 A of the metal in Cu-binding proteins.Journal of the American Society for Mass Spectrometry · 2006Article
- Deciphering structure and topology of conserved COG2042 orphan proteins.BMC structural biology · 2005Article
- Ribosomal protein L7a binds RNA through two distinct RNA-binding domains.The Biochemical journal · 2005Article
- Identification of specific HIV-1 reverse transcriptase contacts to the viral RNA:tRNA complex by mass spectrometry and a primary amine selective reagent.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Chemical cross-linking with thiol-cleavable reagents combined with differential mass spectrometric peptide mapping--a novel approach to assess intermolecular protein contacts.Protein science : a publication of the Protein Society · 2000Article
- Conformational changes in the NS3 protease from hepatitis C virus strain Bk monitored by limited proteolysis and mass spectrometry.Protein science : a publication of the Protein Society · 1999Article
- Engineering of betabellin-15D: a 64 residue beta sheet protein that forms long narrow multimeric fibrils.Protein science : a publication of the Protein Society · 1998Article
- Probing protein structure by amino acid-specific covalent labeling and mass spectrometry.Mass spectrometry reviewsReview
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Abstract
The surface topology of the Minibody, a small de novo-designed beta-protein, has been probed by a strategy that combines selective chemical modification with a variety of reagents and mass spectrometric analysis of the modified fragments. Under appropriate conditions, the susceptibility of individual residues primarily depends on their surface accessibility so that their relative reactivities can be correlated with their position in the tertiary structure of the protein. Moreover, this approach provides information on interacting residues, since intramolecular interactions might greatly affect the reactivity of individual side chains by altering their pKa values. The results of this study indicate that, while overall the Minibody model is correct, the beta-sheet formed by the N- and C-terminal segments is most likely distorted. This is also in agreement with previous results that were obtained using a similar approach where mass spectrometry was used to identify Minibody fragments from limited proteolysis (Zappacosta F, Pessi A, Bianchi E, Venturini S, Sollazzo M, Tramontano A. Marino G, Pucci P. 1996. Probing the tertiary structure of proteins by limited proteolysis and mass spectrometry: The case of Minibody. Protein Sci 5:802-813). The chemical modification approach, in combination with limited proteolysis procedures, can provide useful, albeit partial, structural information to complement simulation techniques. This is especially valuable when, as in the Minibody case, an NMR and/or X-ray structure cannot be obtained due to insufficient solubility of the molecule.
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