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Articles 61 - 69 of 69
Full-Text Articles in Biochemistry
Dioxidobis(2-Oxo-1,2-Dihydropyridin-3-Olato)Molybdenum(Vi), Manoj Trivedi, Daya Pandey, Nigam Rath
Dioxidobis(2-Oxo-1,2-Dihydropyridin-3-Olato)Molybdenum(Vi), Manoj Trivedi, Daya Pandey, Nigam Rath
Chemistry & Biochemistry Faculty Works
In the title compound, [Mo(C5H4NO2)2O2], the MoVI atom exhibits a distorted octahedral coordination geometry formed by two terminal oxo ligands and two monoanionic O,O-bidentate pyridinone ligands. The two terminal oxo ligands lie in a cis arrangement, the ketonic O atoms of the pyridinone ligands are coordinated trans to the oxo ligands and the deprotonated hydroxyl O atoms are located trans to each other. The crystal structure contains intermolecular N-H...O hydrogen bonds, C-H...O contacts and face-to-face [pi]-[pi] stacking interactions with an interplanar separation of 3.25 (1) Å.
Diethyl 2-[(4-NitroPhenYl)(4-Phenyl-1,2,3-Selenadiazol-5-Yl)MethYl]Malonate, A. Marx, S. Saravanan, S. Muthusubramanian, V. Manivannan, Nigam Rath
Diethyl 2-[(4-NitroPhenYl)(4-Phenyl-1,2,3-Selenadiazol-5-Yl)MethYl]Malonate, A. Marx, S. Saravanan, S. Muthusubramanian, V. Manivannan, Nigam Rath
Chemistry & Biochemistry Faculty Works
In the title compound, C22H21N3O6Se, the heterocyclic ring makes dihedral angles of 50.03 (11) and 67.75 (11)°, respectively, with the benzene and phenyl rings. The terminal C atoms of the ester groups are disordered over two positions: the site occupancies for the C atoms are 0.62 (3)/0.38 (3) and 0.48 (3)/0.52 (3). In the crystal structure, weak intra- and intermolecular C-H...O interactions are observed.
4-(4-Chlorophenyl)-5-[1-(4-Chlorophenyl)-2-Methyl-2-Nitropropyl]-1,2,3-Selenadiazole, A. Marx, S. Saravanan, S. Muthusubramanian, V. Manivannan, Nigam Rath
4-(4-Chlorophenyl)-5-[1-(4-Chlorophenyl)-2-Methyl-2-Nitropropyl]-1,2,3-Selenadiazole, A. Marx, S. Saravanan, S. Muthusubramanian, V. Manivannan, Nigam Rath
Chemistry & Biochemistry Faculty Works
In the title compound, C18H15Cl2N3O2Se, the selenadiazole ring makes dihedral angles of 49.87 (3) and 55.70 (3)° with the two benzene rings. The dihedral angle between the two benzene rings is 11.90 (5)°. In the crystal structure, intramolecular C-H...O and C-H...Se interactions and intermolecular C-H...O, C-H...Cl and C-H...N interactions are observed.
Exchange Coupling And Contribution Of Induced Orbital Angular Momentum Of Low-Spin Fe^3+ Ions To Magnetic Anisotropy In Cyanide-Bridged Fe2m2 Molecular Magnets: Spin-Polarized Density-Functional Calculations, Stephen Holmes, Kyungwha Park
Exchange Coupling And Contribution Of Induced Orbital Angular Momentum Of Low-Spin Fe^3+ Ions To Magnetic Anisotropy In Cyanide-Bridged Fe2m2 Molecular Magnets: Spin-Polarized Density-Functional Calculations, Stephen Holmes, Kyungwha Park
Chemistry & Biochemistry Faculty Works
Electronic structure and intramolecular exchange constants are calculated for three cyanide-bridged molecular magnets, [Tp⋆FeIII(CN)3MII(DMF)4]2(OTf)2∙2DMF (MII=Mn,Co,Ni) (abbreviated as Fe2Mn2, Fe2Co2, and Fe2Ni2) that have been recently synthesized, within a generalized-gradient approximation in spin-polarized density-functional theory (DFT). Here Tp⋆=[C3(CH3)2HN2]3BH, OTf=O3SCF3, and DMF=HCON(CH3)2. Due to strong ligand fields present in the [Tp⋆FeIII(CN)3]− units, the Fe3+ ions exhibit a low ground-state spin of S=1/2. Our calculations show that the metal ions in the Fe2Mn2 molecule interact antiferromagnetically via cyanide ligands, while those in the Fe2Co2 and Fe2Ni2 molecule interact ferromagnetically. The calculations also suggest that the smallest gaps between the highest occupied molecular orbital …
[Accepted Article Manuscript Version (Postprint)] Identification And Functional Characterization Of Arabidopsis Peroxin4 And The Interacting Protein Peroxin22, Bethany Zolman, Melanie Monroe-Augustus, Illeana Silva, Bonnie Bartel
[Accepted Article Manuscript Version (Postprint)] Identification And Functional Characterization Of Arabidopsis Peroxin4 And The Interacting Protein Peroxin22, Bethany Zolman, Melanie Monroe-Augustus, Illeana Silva, Bonnie Bartel
Biology Department Faculty Works
Peroxins are genetically defined as proteins necessary for peroxisome biogenesis. By screening for reduced response to indole-3-butyric acid, which is metabolized to active auxin in peroxisomes, we isolated an Arabidopsis thaliana peroxin4 (pex4) mutant. This mutant displays sucrose-dependent seedling development and reduced lateral root production, characteristics of plant peroxisome malfunction. We used yeast two-hybrid analysis to determine that PEX4, an apparent ubiquitinconjugating enzyme, interacts with a previously unidentified Arabidopsis protein, PEX22. A pex4 pex22 double mutant enhanced pex4 defects, confirming that PEX22 is a peroxin. Expression of both Arabidopsis genes together complemented yeast pex4 or pex22 mutant defects, whereas expression …
Metabolic Responses Of Shorebird Chicks To Cold Stress: Hysteresis Of Cooling And Warming Phases, Robert Ricklefs, Joseph Williams
Metabolic Responses Of Shorebird Chicks To Cold Stress: Hysteresis Of Cooling And Warming Phases, Robert Ricklefs, Joseph Williams
Biology Department Faculty Works
We developed a protocol for determining the maximum rate of oxygen consumption of shorebird chicks (Scolopacidae and Charadriidae) in response to cold challenge. We first subjected the chicks to gradually decreasing temperatures until their metabolism peaked and began to decrease. We ended the cooling phase of a trial when a chick’s body temperature Tb had declined typically to 32–34°C. After this point, we gradually increased the temperature in the metabolism chamber until normal Tb values and thermoneutral resting metabolism were restored. We refer to this cycle as the down–up (DU) protocol. We estimated instantaneous oxygen consumption (V . O∑) using …
The Rna-Binding Site Of Bacteriophage Qβ Coat Protein, Francis Lim, Marc Spingola, David Peabody
The Rna-Binding Site Of Bacteriophage Qβ Coat Protein, Francis Lim, Marc Spingola, David Peabody
Biology Department Faculty Works
The coat proteins of the RNA bacteriophages Qβ and MS2 are specific RNA binding proteins. Although they possess common tertiary structures, they bind different RNA stem loops and thus provide useful models of specific protein-RNA recognition. Although the RNA-binding site of MS2 coat protein has been extensively characterized previously, little is known about Qβ. Here we describe the isolation of mutants that define the RNA-binding site of Qβ coat protein, showing that, as with MS2, it resides on the surface of a large β-sheet. Mutations are also described that convert Qβ coat protein to the RNA binding specificity of MS2. …
Conversion Of Bovine Pancreatic Phospholipase A At A Single Site Into A Competitor Of Neurotoxic Phospholipases A By Site-Directed Mutagenesis, Mu-Chin Tzeng, Chon-Ho Yen, Ming-Jhy Hseu, Cynthia M. Dupureur, Ming-Daw Tsai
Conversion Of Bovine Pancreatic Phospholipase A At A Single Site Into A Competitor Of Neurotoxic Phospholipases A By Site-Directed Mutagenesis, Mu-Chin Tzeng, Chon-Ho Yen, Ming-Jhy Hseu, Cynthia M. Dupureur, Ming-Daw Tsai
Educator Preparation & Leadership Faculty Works
A 45-kDa polypeptide preferentially present in neuronal membranes was previously identified as a subunit of a binding (or receptor) protein for several phospholipase A2 variants with neurotoxicity, including crotoxin, by chemical cross-linking experiments (Yen, C.-H., and Tzeng, M.-C.(1991) Biochemistry 30, 11473-11477). The binding of crotoxin to this receptor protein was completely suppressed by sufficient F22Y, a mutated bovine pancreatic phospholipase A2 generated by site-directed mutagenesis of Phe of the wild-type enzyme to Tyr. The IC of this inhibition was estimated to be 1 μM. In sharp contrast, the wild-type enzyme gave no effect even at 50 μM. This …
Altering The Rna Binding Specificity Of A Translational Repressor, F Lim, Marc Spingola, D Peabody
Altering The Rna Binding Specificity Of A Translational Repressor, F Lim, Marc Spingola, D Peabody
Biology Department Faculty Works
The coat proteins of RNA phages MS2 and GA are specific RNA-binding proteins which function to encapsidate viral RNA and to translationally repress synthesis of the viral replicase. The two proteins have highly homologous amino acid sequences, yet they show different RNA binding specificities, recognizing RNA stem-loop structures which differ primarily in the nucleotide sequences of their loops. We sought to convert MS2 coat protein to the RNA binding specificity of GA through the introduction of GA-like amino acid substitutions into the MS2 coat protein RNA-binding site. The effects of the mutations were determined by measuring the affinity of the …