120,884 research outputs found

    Mrs. T. D. Honeyman, Pacific University Board of Trustees member

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    Portrait of Mrs. T. D. Honeyman. She was said to be a board member at Pacific University.[Back] Mrs. Honeyman member Board of Trustees 55768; Notice In publishing this picture proper credit must be given. Photo by BUSHNELL; student and alumni G-H

    Oral memoirs of D. R. Bushnell Jr.: an interview conducted on March 11, 2020

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    Includes interview transcript and photograph.contained in: George Ricks Memorial World War II Oral History ArchiveOriginally recorded in WAV format at 2304 kbps.In this interview, D.R. Bushnell Jr. (b. 1925) relates in detail his experiences growing up in Johnson City, Texas, his time as a radar man in the South Pacific during World War II, and then his life in West Texas following the war. Bushnell rarely ventured far beyond Johnson City as a child, and describes how his parochial worldview was suddenly disrupted in 1943 at the age of 18 by his drafting into the Navy. He first had to report to San Antonio and then was sent by train to San Diego for bootcamp and then San Clemente Island for radar training school. He was then later assigned to an escort aircraft carrier (referred to as a “jeep carrier” or “baby flattop”) that transported planes and supplies to the South Pacific. Following the conclusion of the war, his ship ferried soldiers from Asia and the Pacific back to the United States. Following his service, Bushnell returned to West Texas, where worked at a hardware store and met and married his wife and started a family. They lived in Earth, Muleshoe, Bovina, and then later returned to Johnson City, where they owned a restaurant and antiques business.San Angelo Area Foundatio

    Selenomethionine Incorporation in Saccharomyces cerevisiae RNA Polymerase II

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    AbstractA protocol for the incorporation of SeMet into yeast proteins is described. Incorporation at a level of about 50% suffices for the location of Se sites in an anomalous difference Fourier map of the 0.5 MDa yeast RNA polymerase II. This shows the utility of the approach as an aid in the model-building of large protein complexes

    The influence of drag on human locomotion in water

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    Propulsion in water requires a propulsive force to overcome drag. Male subjects were measured for cycle frequency, energy cost and drag (D) as a function of velocity (V), up to maximal V, for fin and front crawl swimming, kayaking and rowing. The locomotion with the largest propulsive arms and longest hulls traveled the greatest distance per cycle (d/c) and reached higher maximal V. D while locomotoring increased as a function of V, with lower levels for kayaking and rowing at lower Vs. For Vs below 1 m/s, pressure D dominated, while friction D dominated up to 3 m/s, after which wave D dominated total D. Sport training reduced the D, increased d/c, and thus lowered C and increased maximal V. Maximal powers and responses to training were similar in all types of locomotion. To minimize C or maximize V, D has to be minimized by tailoring D type (friction, pressure or wave) to the form of locomotion and velocity. Copyright © 2005 Undersea and Hyperbaric Medical Society, Inc

    Structural basis of transcription: RNA polymerase II at 2.8 Ångstrom resolution

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    Structures of a 10-subunit yeast RNA polymerase II have been derived from two crystal forms at 2.8 and 3.1 angstrom resolution. Comparison of the structures reveals a division of the polymerase into four mobile modules, including a clamp, shown previously to swing over the active center. In the 2.8 angstrom structure, the clamp is in an open state, allowing entry of straight promoter DNA for the initiation of transcription. Three loops extending from the clamp may play roles in RNA unwinding and DNA rewinding during transcription. A 2.8 angstrom difference Fourier map reveals two metal ions at the active site, one persistently bound and the other possibly exchangeable during RNA synthesis. The results also provide evidence for RNA exit in the vicinity of the carboxyl-terminal repeat domain, coupling synthesis to RNA processing by enzymes bound to this domain

    Structural basis of transcription: α-Amanitin–RNA polymerase II cocrystal at 2.8 Å resolution

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    The structure of RNA polymerase II in a complex with the inhibitor α-amanitin has been determined by x-ray crystallography. The structure of the complex indicates the likely basis of inhibition and gives unexpected insight into the transcription mechanism

    Grain Elevator, Bushnell SD, Brookings County

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    4 x 6 photograph, grain elevator with a gable roof cupola next to a tall building with a gable roof and a garage door with a slanted roof on the sideH2010-041 Elevators School Houses Courthouses Vernell Johnson Coll. Box 3 SD Elevators[stamp] 348 [photographer stamp] Photo By: Vernell Johnson, S. D. Bushnell, S. D

    Energy balance of human locomotion in water

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    In this paper a complete energy balance for water locomotion is attempted with the aim of comparing different modes of transport in the aquatic environment (swimming underwater with SCUBA diving equipment, swimming at the surface: leg kicking and front crawl, kayaking and rowing). On the basis of the values of metabolic power (E), of the power needed to overcome water resistance (W-d) and of propelling efficiency (eta(P)=W-d/W-tot, where W-tot is the total mechanical power) as reported in the literature for each of these forms of locomotion, the energy cost per unit distance (C=E/v, where v is the velocity), the drag (performance) efficiency (eta(d)=W-d/E) and the overall efficiency (eta(o)=W-tot/E=eta(d)/eta(P)) were calculated. As previously found for human locomotion on land, for a given metabolic power (e.g. 0.5 kW=1.43 l.min(-1) VO2) the decrease in C (from 0.88 kJ.m(-1) in SCUBA diving to 0.22 kJ.m(-1) in rowing) is associated with an increase in the speed of locomotion (from 0.6 m.s(-1) in SCUBA diving to 2.4 m.s(-1) in rowing). At variance with locomotion on land, however, the decrease in C is associated with an increase, rather than a decrease, of the total mechanical work per unit distance (W-tot, kJ.m(-1)). This is made possible by the increase of the overall efficiency of locomotion (eta(o)=W-tot/E=W-tot/C) from the slow speeds (and loads) of swimming to the high speeds (and loads) attainable with hulls and boats (from 0.10 in SCUBA diving to 0.29 in rowing)

    Structural basis of transcription: An RNA polymerase II elongation complex at 3.3 Å resolution

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    The crystal structure of RNA polymerase II in the act of transcription was determined at 3.3  resolution. Duplex DNA is seen entering the main cleft of the enzyme and unwinding before the active site. Nine base pairs of DNA-RNA hybrid extend from the active center at nearly right angles to the entering DNA, with the 39 end of the RNA in the nucleotide addition site. The 39 end is positioned above a pore, through which nucleotides may enter and through which RNA may be extruded during back-tracking. The 59-most residue of the RNA is close to the point of entry to an exit groove. Changes in protein structure between the transcribing complex and free enzyme include closure of a clamp over the DNA and RNA and ordering of a series of ÒswitchesÓ at the base of the clamp to create a binding site complementary to the DNA-RNA hybrid. ProteinÐ nucleic acid contacts help explain DNA and RNA strand separation, the speci Þcity of RNA synthesis, Òabortive cyclingÓ during transcription initiation, and RNA and DNA translocation during transcription elongation

    A. D. Fricke, author

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    Black and white photograph of author, A. D. Fricke
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