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Relative interfacial cleavage energetics of protein complexes revealed by surface collisions.
Harvey, Sophie R; Seffernick, Justin T; Quintyn, Royston S; Song, Yang; Ju, Yue; Yan, Jing; Sahasrabuddhe, Aniruddha N; Norris, Andrew; Zhou, Mowei; Behrman, Edward J; Lindert, Steffen; Wysocki, Vicki H.
Afiliação
  • Harvey SR; Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.
  • Seffernick JT; Resource for Native Mass Spectrometry Guided Structural Biology, The Ohio State University, Columbus, OH 43210.
  • Quintyn RS; Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.
  • Song Y; Resource for Native Mass Spectrometry Guided Structural Biology, The Ohio State University, Columbus, OH 43210.
  • Ju Y; Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.
  • Yan J; Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.
  • Sahasrabuddhe AN; Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.
  • Norris A; Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.
  • Zhou M; Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.
  • Behrman EJ; Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.
  • Lindert S; Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.
  • Wysocki VH; Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210.
Proc Natl Acad Sci U S A ; 116(17): 8143-8148, 2019 04 23.
Article em En | MEDLINE | ID: mdl-30944216
To fulfill their biological functions, proteins must interact with their specific binding partners and often function as large assemblies composed of multiple proteins or proteins plus other biomolecules. Structural characterization of these complexes, including identification of all binding partners, their relative binding affinities, and complex topology, is integral for understanding function. Understanding how proteins assemble and how subunits in a complex interact is a cornerstone of structural biology. Here we report a native mass spectrometry (MS)-based method to characterize subunit interactions in globular protein complexes. We demonstrate that dissociation of protein complexes by surface collisions, at the lower end of the typical surface-induced dissociation (SID) collision energy range, consistently cleaves the weakest protein:protein interfaces, producing products that are reflective of the known structure. We present here combined results for multiple complexes as a training set, two validation cases, and four computational models. We show that SID appearance energies can be predicted from structures via a computationally derived expression containing three terms (number of residues in a given interface, unsatisfied hydrogen bonds, and a rigidity factor).
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas Tipo de estudo: Prognostic_studies Idioma: En Ano de publicação: 2019 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas Tipo de estudo: Prognostic_studies Idioma: En Ano de publicação: 2019 Tipo de documento: Article