Proteins fold into three-dimensional structures, and the structure dictates the function of the proteins. Further, proteins interact in a multitude of ways, ranging from transient interactions to forming protein complexes that are stable over time. Hence, understanding biological systems will ultimately depend on knowing the structure of, ideally, all individual proteins, and how they interact to form higher-order structures.
My research uses protein structure modeling and distance constraints derived from chemical cross-linking mass spectrometry to determine protein complex structures, measured directly in unfractionated, biologically relevant samples.
|2.||Drew, Kevin; Winters, Patrick; Butterfoss, Glenn; Berstis, Viktors; Uplinger, Keith; Armstrong, Jonathan; Riffle, Michael; Schweighofer, Erik; Bovermann, Bill; Goodlett, David; Davis, Trisha; Shasha, Dennis; Malmstrom, Lars; Bonneau, Richard; The proteome folding project: Proteome-scale prediction of structure and function. Genome Res (2011), 21: 1981-94.|
|1.||Malmstrom, Lars; Riffle, Michael; Strauss, Charlie; Chivian, Dylan; Davis, Trisha; Bonneau, Richard; Baker, David; Superfamily Assignments for the Yeast Proteome through Integration of Structure Prediction with the Gene Ontology. PLoS Biol (2007), 5: e76.|