1. Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser.

    Nature 523(7562):561 (2015) PMID 26200343 PMCID PMC4521999

    G-protein-coupled receptors (GPCRs) signal primarily through G proteins or arrestins. Arrestin binding to GPCRs blocks G protein interaction and redirects signalling to numerous G-protein-independent pathways. Here we report the crystal structure of a constitutively active form of human rhodopsi...
  2. SIGNAL TRANSDUCTION. Structural basis for nucleotide exchange in heterotrimeric G proteins.

    Science 348(6241):1361 (2015) PMID 26089515

    G protein-coupled receptors (GPCRs) relay diverse extracellular signals into cells by catalyzing nucleotide release from heterotrimeric G proteins, but the mechanism underlying this quintessential molecular signaling event has remained unclear. Here we use atomic-level simulations to elucidate t...
  3. Structural Insights into the Dynamic Process of β2-Adrenergic Receptor Signaling.

    Cell 161(5):1101 (2015) PMID 25981665 PMCID PMC4441853

    G-protein-coupled receptors (GPCRs) transduce signals from the extracellular environment to intracellular proteins. To gain structural insight into the regulation of receptor cytoplasmic conformations by extracellular ligands during signaling, we examine the structural dynamics of the cytoplasmi...
  4. Structure-relaxation mechanism for the response of T4 lysozyme cavity mutants to hydrostatic pressure.

    PNAS 112(19):E2437 (2015) PMID 25918400 PMCID PMC4434698

    Application of hydrostatic pressure shifts protein conformational equilibria in a direction to reduce the volume of the system. A current view is that the volume reduction is dominated by elimination of voids or cavities in the protein interior via cavity hydration, although an alternative mecha...
  5. The guanine nucleotide exchange factor Ric-8A induces domain separation and Ras domain plasticity in Gαi1.

    PNAS 112(5):1404 (2015) PMID 25605908

    Heterotrimeric G proteins are activated by exchange of GDP for GTP at the G protein alpha subunit (Gα), most notably by G protein-coupled transmembrane receptors. Ric-8A is a soluble cytoplasmic protein essential for embryonic development that acts as both a guanine nucleotide exchange factor (G...
  6. The guanine nucleotide exchange factor Ric-8A induces domain separation and Ras domain plasticity in Gαi1.

    PNAS 112(5):1404 (2015) PMID 25605908 PMCID PMC4321267

    Heterotrimeric G proteins are activated by exchange of GDP for GTP at the G protein alpha subunit (Gα), most notably by G protein-coupled transmembrane receptors. Ric-8A is a soluble cytoplasmic protein essential for embryonic development that acts as both a guanine nucleotide exchange factor (G...
  7. The guanine nucleotide exchange factor Ric-8A induces domain separation and Ras domain plasticity in Gαi1.

    PNAS 112(5):1404 (2015) PMID 25605908 PMCID PMC4321267

    Heterotrimeric G proteins are activated by exchange of GDP for GTP at the G protein alpha subunit (Gα), most notably by G protein-coupled transmembrane receptors. Ric-8A is a soluble cytoplasmic protein essential for embryonic development that acts as both a guanine nucleotide exchange factor (G...
  8. Differential dynamics of extracellular and cytoplasmic domains in denatured States of rhodopsin.

    Biochemistry (Washington) 53(46):7160 (2014) PMID 25268658 PMCID PMC4245987

    Rhodopsin is a model system for understanding membrane protein folding. Recently, conditions that allow maximally denaturing rhodopsin without causing aggregation have been determined, opening the door to the first structural characterization of denatured states of rhodopsin by nuclear magnetic ...
  9. Differential dynamics of extracellular and cytoplasmic domains in denatured States of rhodopsin.

    Biochemistry (Washington) 53(46):7160 (2014) PMID 25268658 PMCID PMC4245987

    Rhodopsin is a model system for understanding membrane protein folding. Recently, conditions that allow maximally denaturing rhodopsin without causing aggregation have been determined, opening the door to the first structural characterization of denatured states of rhodopsin by nuclear magnetic ...
  10. Differential dynamics of extracellular and cytoplasmic domains in denatured States of rhodopsin.

    Biochemistry (Washington) 53(46):7160 (2014) PMID 25268658 PMCID PMC4245987

    Rhodopsin is a model system for understanding membrane protein folding. Recently, conditions that allow maximally denaturing rhodopsin without causing aggregation have been determined, opening the door to the first structural characterization of denatured states of rhodopsin by nuclear magnetic ...
  11. Differential dynamics of extracellular and cytoplasmic domains in denatured States of rhodopsin.

    Biochemistry (Washington) 53(46):7160 (2014) PMID 25268658 PMCID PMC4245987

    Rhodopsin is a model system for understanding membrane protein folding. Recently, conditions that allow maximally denaturing rhodopsin without causing aggregation have been determined, opening the door to the first structural characterization of denatured states of rhodopsin by nuclear magnetic ...
  12. Differential dynamics of extracellular and cytoplasmic domains in denatured States of rhodopsin.

    Biochemistry (Washington) 53(46):7160 (2014) PMID 25268658 PMCID PMC4245987

    Rhodopsin is a model system for understanding membrane protein folding. Recently, conditions that allow maximally denaturing rhodopsin without causing aggregation have been determined, opening the door to the first structural characterization of denatured states of rhodopsin by nuclear magnetic ...
  13. Stationary-phase EPR for exploring protein structure, conformation, and dynamics in spin-labeled proteins.

    Biochemistry (Washington) 53(45):7067 (2014) PMID 25333901 PMCID PMC4238802

    Proteins tethered to solid supports are of increasing interest in bioanalytical chemistry and protein science in general. However, the extent to which tethering modifies the energy landscape and dynamics of the protein is most often unknown because there are few biophysical methods that can dete...
  14. Stationary-phase EPR for exploring protein structure, conformation, and dynamics in spin-labeled proteins.

    Biochemistry (Washington) 53(45):7067 (2014) PMID 25333901 PMCID PMC4238802

    Proteins tethered to solid supports are of increasing interest in bioanalytical chemistry and protein science in general. However, the extent to which tethering modifies the energy landscape and dynamics of the protein is most often unknown because there are few biophysical methods that can dete...
  15. Stationary-phase EPR for exploring protein structure, conformation, and dynamics in spin-labeled proteins.

    Biochemistry (Washington) 53(45):7067 (2014) PMID 25333901 PMCID PMC4238802

    Proteins tethered to solid supports are of increasing interest in bioanalytical chemistry and protein science in general. However, the extent to which tethering modifies the energy landscape and dynamics of the protein is most often unknown because there are few biophysical methods that can dete...
  16. Stationary-Phase EPR for Exploring Protein Structure, Conformation, and Dynamics in Spin-Labeled Proteins.

    Biochemistry (Washington) 53(45):7067 (2014) PMID 25333901 PMCID PMC4238802

    Proteins tethered to solid supports are of increasing interest in bioanalytical chemistry and protein science in general. However, the extent to which tethering modifies the energy landscape and dynamics of the protein is most often unknown because there are few biophysical methods that can dete...
  17. Stationary-phase EPR for exploring protein structure, conformation, and dynamics in spin-labeled proteins.

    Biochemistry (Washington) 53(45):7067 (2014) PMID 25333901 PMCID PMC4238802

    Proteins tethered to solid supports are of increasing interest in bioanalytical chemistry and protein science in general. However, the extent to which tethering modifies the energy landscape and dynamics of the protein is most often unknown because there are few biophysical methods that can dete...
  18. 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...
  19. 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...
  20. 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...