1. Long-range distance measurements in proteins at physiological temperatures using saturation recovery EPR spectroscopy.

    Journal of the American Chemical Society 136(43):15356 (2014) PMID 25290172 PMCID PMC4227719

    Site-directed spin labeling in combination with EPR is a powerful method for providing distances on the nm scale in biological systems. The most popular strategy, double electron-electron resonance (DEER), is carried out at cryogenic temperatures (50-80 K) to increase the short spin-spin relaxat...
  2. Long-range distance measurements in proteins at physiological temperatures using saturation recovery EPR spectroscopy.

    Journal of the American Chemical Society 136(43):15356 (2014) PMID 25290172 PMCID PMC4227719

    Site-directed spin labeling in combination with EPR is a powerful method for providing distances on the nm scale in biological systems. The most popular strategy, double electron-electron resonance (DEER), is carried out at cryogenic temperatures (50-80 K) to increase the short spin-spin relaxat...
  3. Long-range distance measurements in proteins at physiological temperatures using saturation recovery EPR spectroscopy.

    Journal of the American Chemical Society 136(43):15356 (2014) PMID 25290172 PMCID PMC4227719

    Site-directed spin labeling in combination with EPR is a powerful method for providing distances on the nm scale in biological systems. The most popular strategy, double electron-electron resonance (DEER), is carried out at cryogenic temperatures (50-80 K) to increase the short spin-spin relaxat...
  4. Long-Range Distance Measurements in Proteins at Physiological Temperatures Using Saturation Recovery EPR Spectroscopy.

    Journal of the American Chemical Society 136(43):15356 (2014) PMID 25290172 PMCID PMC4227719

    Site-directed spin labeling in combination with EPR is a powerful method for providing distances on the nm scale in biological systems. The most popular strategy, double electron-electron resonance (DEER), is carried out at cryogenic temperatures (50-80 K) to increase the short spin-spin relaxat...
  5. Structural and energetic determinants of adhesive binding specificity in type I cadherins.

    PNAS 111(40):E4175 (2014) PMID 25253890 PMCID PMC4210030

    Type I cadherin cell-adhesion proteins are similar in sequence and structure and yet are different enough to mediate highly specific cell-cell recognition phenomena. It has previously been shown that small differences in the homophilic and heterophilic binding affinities of different type I fami...
  6. Structural and energetic determinants of adhesive binding specificity in type I cadherins.

    PNAS 111(40):E4175 (2014) PMID 25253890 PMCID PMC4210030

    Type I cadherin cell-adhesion proteins are similar in sequence and structure and yet are different enough to mediate highly specific cell-cell recognition phenomena. It has previously been shown that small differences in the homophilic and heterophilic binding affinities of different type I fami...
  7. Structural and energetic determinants of adhesive binding specificity in type I cadherins.

    PNAS 111(40):E4175 (2014) PMID 25253890 PMCID PMC4210030

    Type I cadherin cell-adhesion proteins are similar in sequence and structure and yet are different enough to mediate highly specific cell-cell recognition phenomena. It has previously been shown that small differences in the homophilic and heterophilic binding affinities of different type I fami...
  8. Structural and energetic determinants of adhesive binding specificity in type I cadherins.

    PNAS 111(40):E4175 (2014) PMID 25253890 PMCID PMC4210030

    Type I cadherin cell-adhesion proteins are similar in sequence and structure and yet are different enough to mediate highly specific cell-cell recognition phenomena. It has previously been shown that small differences in the homophilic and heterophilic binding affinities of different type I fami...
  9. Identification of a unique Fe-S cluster binding site in a glycyl-radical type microcompartment shell protein.

    Journal of Molecular Biology 426(19):3287 (2014) PMID 25102080 PMCID PMC4175982

    Recently, progress has been made toward understanding the functional diversity of bacterial microcompartment (MCP) systems, which serve as protein-based metabolic organelles in diverse microbes. New types of MCPs have been identified, including the glycyl-radical propanediol (Grp) MCP. Within th...
  10. Identification of a unique Fe-S cluster binding site in a glycyl-radical type microcompartment shell protein.

    Journal of Molecular Biology 426(19):3287 (2014) PMID 25102080 PMCID PMC4175982

    Recently, progress has been made toward understanding the functional diversity of bacterial microcompartment (MCP) systems, which serve as protein-based metabolic organelles in diverse microbes. New types of MCPs have been identified, including the glycyl-radical propanediol (Grp) MCP. Within th...
  11. Identification of a unique Fe-S cluster binding site in a glycyl-radical type microcompartment shell protein.

    Journal of Molecular Biology 426(19):3287 (2014) PMID 25102080 PMCID PMC4175982

    Recently, progress has been made toward understanding the functional diversity of bacterial microcompartment (MCP) systems, which serve as protein-based metabolic organelles in diverse microbes. New types of MCPs have been identified, including the glycyl-radical propanediol (Grp) MCP. Within th...
  12. Identification of a Unique Fe-S Cluster Binding Site in a Glycyl-Radical Type Microcompartment Shell Protein

    Journal of Molecular Biology 426(19):3287 (2014)

    Recently, progress has been made toward understanding the functional diversity of bacterial microcompartment (MCP) systems, which serve as protein-based metabolic organelles in diverse microbes. New types of MCPs have been identified, including the glycyl-radical propanediol (Grp) MCP....
  13. Identification of a unique Fe-S cluster binding site in a glycyl-radical type microcompartment shell protein.

    Journal of Molecular Biology 426(19):3287 (2014) PMID 25102080 PMCID PMC4175982

    Recently, progress has been made toward understanding the functional diversity of bacterial microcompartment (MCP) systems, which serve as protein-based metabolic organelles in diverse microbes. New types of MCPs have been identified, including the glycyl-radical propanediol (Grp) MCP. Within th...
  14. Identification of a unique Fe-S cluster binding site in a glycyl-radical type microcompartment shell protein.

    Journal of Molecular Biology 426(19):3287 (2014) PMID 25102080 PMCID PMC4175982

    Recently, progress has been made toward understanding the functional diversity of bacterial microcompartment (MCP) systems, which serve as protein-based metabolic organelles in diverse microbes. New types of MCPs have been identified, including the glycyl-radical propanediol (Grp) MCP. Within th...
  15. Mapping protein conformational heterogeneity under pressure with site-directed spin labeling and double electron-electron resonance.

    PNAS 111(13):E1201 (2014) PMID 24707053 PMCID PMC3977274

    The dominance of a single native state for most proteins under ambient conditions belies the functional importance of higher-energy conformational states (excited states), which often are too sparsely populated to allow spectroscopic investigation. Application of high hydrostatic pressure increa...
  16. Mapping protein conformational heterogeneity under pressure with site-directed spin labeling and double electron-electron resonance.

    PNAS 111(13):E1201 (2014) PMID 24707053 PMCID PMC3977274

    The dominance of a single native state for most proteins under ambient conditions belies the functional importance of higher-energy conformational states (excited states), which often are too sparsely populated to allow spectroscopic investigation. Application of high hydrostatic pressure increa...
  17. Mapping protein conformational heterogeneity under pressure with site-directed spin labeling and double electron-electron resonance.

    PNAS 111(13):E1201 (2014) PMID 24707053 PMCID PMC3977274

    The dominance of a single native state for most proteins under ambient conditions belies the functional importance of higher-energy conformational states (excited states), which often are too sparsely populated to allow spectroscopic investigation. Application of high hydrostatic pressure increa...
  18. Structural and Energetic Determinants of Adhesive Binding Specificity in Type I Cadherins: The Role of Multiple Conformations in Tuning Affinities

    Biophysical Journal 106(2):464a (2014)

  19. Technological advances in site-directed spin labeling of proteins.

    Current Opinion in Structural Biology 23(5):725 (2013) PMID 23850140 PMCID PMC3805720

    Molecular flexibility over a wide time range is of central importance to the function of many proteins, both soluble and membrane. Revealing the modes of flexibility, their amplitudes, and time scales under physiological conditions is the challenge for spectroscopic methods, one of which is site...
  20. Technological advances in site-directed spin labeling of proteins.

    Current Opinion in Structural Biology 23(5):725 (2013) PMID 23850140 PMCID PMC3805720

    Molecular flexibility over a wide time range is of central importance to the function of many proteins, both soluble and membrane. Revealing the modes of flexibility, their amplitudes, and time scales under physiological conditions is the challenge for spectroscopic methods, one of which is site...