A5007117025- Biotin and Related Studies
- Enzyme Structure and Function
- Click Chemistry and Applications
- Photoreceptor and optogenetics research
- Receptor Mechanisms and Signaling
- Metal-Catalyzed Oxygenation Mechanisms
- Hemoglobin structure and function
- Protein Structure and Dynamics
- Molecular Junctions and Nanostructures
- Metal complexes synthesis and properties
- Glutathione Transferases and Polymorphisms
- Photosynthetic Processes and Mechanisms
- Monoclonal and Polyclonal Antibodies Research
- Magnetism in coordination complexes
- Blood properties and coagulation
- RNA and protein synthesis mechanisms
- Molecular spectroscopy and chirality
- Neuroscience and Neuropharmacology Research
- Porphyrin Metabolism and Disorders
- Carbohydrate Chemistry and Synthesis
- Bacterial Genetics and Biotechnology
- Chemical Synthesis and Analysis
- Genomics, phytochemicals, and oxidative stress
- Cyclopropane Reaction Mechanisms
- Crystal structures of chemical compounds
University of Washington
2010-2022
Vanderbilt University
2008
Ocular Surface Center
2007
GTx (United States)
2006
Seattle University
1983-2005
University of Warsaw
2003
Kansas State University
1998
Institute of Molecular Biology and Biophysics
1996
European Synchrotron Radiation Facility
1996
European Molecular Biology Laboratory
1996
Heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors (GPCRs) respond to a variety of different external stimuli and activate G proteins. GPCRs share many structural features, including bundle seven transmembrane alpha helices connected by six loops varying lengths. We determined the structure rhodopsin from diffraction data extending 2.8 angstroms resolution. The highly organized in extracellular region, conserved disulfide bridge, forms basis for arrangement...
The changes that lead to activation of G protein-coupled receptors have not been elucidated at the structural level. In this work we report crystal structures both ground state and a photoactivated deprotonated intermediate bovine rhodopsin resolution 4.15 A. state, Schiff base linking chromophore Lys-296 becomes deprotonated, reminiscent protein-activating metarhodopsin II. reveal accompany photoactivation are smaller than previously predicted for II include on cytoplasmic surface possibly...
Mechanical stability in many biological materials is provided by the crosslinking of large structural proteins with gamma-glutamyl-epsilon-lysyl amide bonds. The three-dimensional structure human recombinant factor XIII (EC 2.3.2.13 zymogen; protein-glutamine:amine gamma-glutamyltransferase a chain), transglutaminase zymogen, has been solved at 2.8-A resolution x-ray crystallography. This shows that each chain homodimeric protein folded into four sequential domains. A catalytic triad...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTBinuclear iron complexes in methemerythrin and azidomethemerythrin at 2.0-.ANG. resolutionRonald E. Stenkamp, Larry C. Sieker, Lyle H. JensenCite this: J. Am. Chem. Soc. 1984, 106, 3, 618–622Publication Date (Print):February 1, 1984Publication History Published online1 May 2002Published inissue 1 February 1984https://pubs.acs.org/doi/10.1021/ja00315a027https://doi.org/10.1021/ja00315a027research-articleACS PublicationsRequest reuse...
A structure is worth a thousand words: Guided by the X-ray of an S-selective artificial transfer hydrogenase, designed evolution was used to optimize selectivity hybrid catalysts. Fine-tuning second coordination sphere ruthenium center (see picture, orange sphere) introduction two point mutations allowed identification selective hydrogenases for reduction dialkyl ketones.
After vascular injury, a cascade of serine protease activations leads to the conversion soluble fibrinogen molecule into fibrin. The fibrin monomers then polymerize spontaneously and noncovalently form gel. primary interaction this polymerization reaction is between newly exposed N-terminal Gly-Pro-Arg sequence α chain one C-terminal region γ an adjacent fibrin(ogen) molecule. In report, pocket has been identified by determining crystal structure 30-kDa fragment complexed with peptide...
The thermodynamic and structural cooperativity between the Ser45- D128-biotin hydrogen bonds was measured by calorimetric X-ray crystallographic studies of S45A/D128A double mutant streptavidin. exhibits a binding affinity approximately 2x10(7) times lower than that wild-type streptavidin at 25 degrees C. corresponding reduction in free energy (DeltaDeltaG) 10.1 kcal/mol nearly completely due to enthalpy losses this temperature. loss is 11-fold greater predicted linear combination...
Abstract The X‐ray crystal structure of human transglutaminase factor XIII has revealed a cysteine proteinase‐like active site involved in crosslinking reaction and not proteolysis. This is among the first observations similar sites 2 different enzyme families catalyzing opposite directions. Although size overall protein fold proteinases are quite different, surrounding share structural features suggesting common evolutionary lineage. Here we present description residues evidence that...
A major question in G protein-coupled receptor signaling concerns the quaternary structure required for signal transduction. Do these transmembrane receptors function as monomers, dimers, or larger oligomers? We have investigated oligomeric state of model rhodopsin (Rho), which absorbs light and initiates a phototransduction-signaling cascade that forms basis vision. In this study, different Rho were isolated using gel filtration techniques mild detergents, including...
Rhodopsin (Rho) is a G protein-coupled receptor that initiates phototransduction in rod photoreceptors. High expression levels of Rho the disc membranes outer segments and propensity to form higher oligomeric structures are evident from atomic force microscopy, transmission electron chemical cross-linking experiments. To explore structural functional properties n-dodecyl-beta-maltoside, frequently used purify heterologously expressed its mutants, we gel filtration techniques, blue native...