Filters: School Or College: "College of Pharmacy" Collection: "ir_uspace" Department: "Medicinal Chemistry"
1 - 25 of 8
| Creator | Title | Description | Subject | Date | ||
|---|---|---|---|---|---|---|
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Poulter, Charles Dale | Isopentenyl diphosphate:dimethylallyl diphosphate isomerase. An improved purification of the enzyme and isolation of the gene from Saccharomyces cerevisiae. | Isopentenyl diphosphate:dimethylallyl diphosphate isomerase (IPP isomerase) is an enzyme in the isoprenoid biosynthetic pathway which catalyzes the interconversion of the primary five-carbon homoallylic and allylic diphosphate building blocks. We report a substantially improved procedure for purific... | Amino Acid Sequence; Base Sequence; Chromatography, Gel; Chromatography, Ion Exchange | 1989-11-15 |
| 2 |
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Poulter, Charles Dale; Davis, Darrell R. | 15N labeled e. coli tRNAMet, tRNAGlu, tRNATyr, and tRNAPhe. Double resonance and two dimensional NMR of H-N1 units in pseudouridine | The N1 imino units in Escherichia coli tRNAfMet, tRNAGlu, tRNAPhe, and tRNATyr were studied by 1H-15N NMR using three different techniques to suppress signals of protons not attached to 15N. Two of the procedures, Fourier internuclear difference spectroscopy and two-dimensional forbidden echo spectr... | Escherichia coli; Magnetic resonance spectroscopy; Nucleic acid conformation | 1985-08-15 |
| 3 |
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Poulter, Charles Dale; Davis, Darrell R. | 15N-labeled tRNA. Identification of dihydrouridine in Escherichia coli tRNAfMet, tRNALys, and tRNAPhe by 1H-15N two-dimensional NMR. | The N3 imino units of dihydrouridine were identified in samples of 15N-labeled Escherichia coli tRNAfMet, tRNALys, and tRNAPhe by 1H-15N two-dimensional NMR. The peaks for dihydrouridine had high field 1H (9.7-9.8 ppm) and 15N (147.8-149.5 ppm) chemical shifts. Assignments were made by 1H-15N chemic... | Hydrogen Bonding; Magnetic Resonance Spectroscopy; Magnetic Resonance Spectroscopy | 1986-03-15 |
| 4 |
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Poulter, Charles Dale | Farnesyl pyrophosphate synthetase. Mechanistic studies of the 1'-4 coupling reaction with 2-fluorogeranyl pyrophosphate. | The mechanism of the 1'-4 coupling reaction between isopentenyl pyrophosphate and geranyl pyrophosphate catalyzed by farnesyl pyrophosphate synthetase from porcine liver was studied with the allylic substrate analogue 2-fluorogeranyl pyrophosphate. 2-Fluorogeranyl pyrophosphate is an alternate subst... | Kinetics; Liver; Mass Spectrometry; Organophosphorus Compounds; Protein Binding | 1978-10-25 |
| 5 |
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Baehr, Wolfgang; Prestwich, Glenn D. | Photoreceptor cGMP phosphodiesterase delta subunit (PDEdelta) functions as a prenyl-binding protein | Bovine PDEdelta was originally copurified with rod cGMP phosphodiesterase (PDE) and shown to interact with prenylated, carboxymethylated C-terminal Cys residues. Other studies showed that PDEdelta can interact with several small GTPases including Rab13, Ras, Rap, and Rho6, all of which are prenylate... | Fluorescence Resonance Energy Transfer; GTP Phosphohydrolases; Immunohistochemistry | 2004 |
| 6 |
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Poulter, Charles Dale | Prenyltransferase. Kinetic studies of the 1'-4 coupling reaction with avian liver enzyme. | Prenyltransferase catalyzes the sequential, irreversible 1'-4 condensation of isopentenyl-PP with dimethylallyl-PP and geranyl-PP to yield farnesyl-PP. A kinetic study shows substrate inhibition by isopentenyl-PP at concentrations above 0.7 microM when the concentration of geranyl-PP is 1.0 microM o... | Birds; Kinetics; Structure-Activity Relationship; Substrate Specificity | 1979-10-10 |
| 7 |
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Poulter, Charles Dale; Davis, Darrell R. | 15N-labeled Escherichia coli tRNAfMet, tRNAGlu, tRNATyr, and tRNAPhe. Double resonance and two-dimensional NMR of N1-labeled pseudouridine. | The N1 imino units in Escherichia coli tRNAfMet, tRNAGlu, tRNAPhe, and tRNATyr were studied by 1H-15N NMR using three different techniques to suppress signals of protons not attached to 15N. Two of the procedures, Fourier internuclear difference spectroscopy and two-dimensional forbidden echo spectr... | Escherichia coli; Magnetic resonance spectroscopy; Nitrogen; Nucleic acid conformation | 1985-08-15 |
| 8 |
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Poulter, Charles Dale; Davis, Darrell R. | 15N-labeled tRNA. Identification of 4-thiouridine in Escherichia coli tRNASer1 and tRNATyr2 by 1H-15N two-dimensional NMR spectroscopy. | Uridine is uniquely conserved at position 8 in elongator tRNAs and binds to A14 to form a reversed Hoogsteen base pair which folds the dihydrouridine loop back into the core of the L-shaped molecule. On the basis of 1H NMR studies, Hurd and co-workers (Hurd, R. E., Robillard, G. T., and Reid, B. R. ... | Magnetic resonance spectroscopy | 1986-09-15 |
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