89 research outputs found

    iAt Book Club: How to Think

    Get PDF
    This book club series features the book, How to Think: A Survival Guide for a World at Odds, by Alan Jacobs. Various voices have contributed to the series as they interacted with one another and responded to the book. Series contributors are Erin Olson, Mary Nickel, Myles Werntz, and Justin Bailey. Access at publisher\u27s site: https://inallthings.org/iat-book-club-how-to-think-round-table-2

    Accurate Acoustic 2D Mapping Apparatus

    Full text link
    ME450 Capstone Design and Manufacturing Experience: Fall 2020Prof. Popa's lab has an acoustic mapping chamber used in his experiments on metamaterials. The current microphone positioning system interferes with data collection. The purpose of this project was to develop a positioning system that acts without direct connection to the interior of the chamber. Our design process resulted in a magnetically positioned interior housing that can easily interface with the existing setup. Pandemic restrictions and time constraints prevented us from completing a prototype housing, but our empirical testing of a simple mockup did show promising results.Prof. Bogdan Popa, U-M Mechanical Engineering - Popa Research Grouphttp://deepblue.lib.umich.edu/bitstream/2027.42/164451/1/Accurate_Acoustic_2D_Mapping_Apparatus.pd

    Heme ligation and redox chemistry in two bacterial thiosulfate dehydrogenase (TsdA) enzyme

    Get PDF
    Thiosulfate dehydrogenases (TsdA) are bidirectional bacterial di-heme enzymes that catalyze the interconversion of tetrathionate and thiosulfate at measurable rates in both directions. In contrast to our knowledge of TsdA activities, information on the redox properties in the absence of substrates is rather scant. To address this deficit, we combined magnetic circular dichroism (MCD) spectroscopy and protein film electrochemistry (PFE) in a study to resolve heme ligation and redox chemistry in two representative TsdAs. We examined the TsdAs from Campylobacter jejuni, a micro-aerobe human pathogen, and from the purple sulfur bacterium Allochromatium vinosum. In these organisms, the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase respectively. The active site Heme 1 in both enzymes has His/Cys− ligation in the ferric and ferrous states and the midpoint potentials (Em) of the corresponding redox transformations are similar, −185 mV versus standard hydrogen electrode (SHE). However, fundamental differences are observed in the properties of the second, electron transferring, Heme 2. In C. jejuni TsdA Heme 2 has His/Met ligation and an Em of +172 mV. In A. vinosum TsdA, Heme 2 reduction triggers a switch from His/Lys ligation (Em, −129 mV) to His/Met (Em,+266 mV) but the rates of interconversion are such that His/Lys ligation would be retained during turnover. In summary, our findings have unambiguously assigned Em values to defined axial ligand sets in TsdAs, specified the rates of Heme 2 ligand exchange in the A. vinosum enzyme, and provided information relevant to describing their catalytic mechanism(s)

    Electrochemical titrations and reaction time courses monitored in situ by magnetic circular dichroism spectroscopy

    Get PDF
    Magnetic circular dichroism (MCD) spectra, at ultraviolet–visible or near-infrared wavelengths (185–2000 nm), contain the same transitions observed in conventional absorbance spectroscopy, but their bisignate nature and more stringent selection rules provide greatly enhanced resolution. Thus, they have proved to be invaluable in the study of many transition metal-containing proteins. For mainly technical reasons, MCD has been limited almost exclusively to the measurement of static samples. But the ability to employ the resolving power of MCD to follow changes at transition metal sites would be a potentially significant advance. We describe here the development of a cuvette holder that allows reagent injection and sample mixing within the 50-mm-diameter ambient temperature bore of an energized superconducting solenoid. This has allowed us, for the first time, to monitor time-resolved MCD resulting from in situ chemical manipulation of a metalloprotein sample. Furthermore, we report the parallel development of an electrochemical cell using a three-electrode configuration with physically separated working and counter electrodes, allowing true potentiometric titration to be performed within the bore of the MCD solenoid

    Miniature exoplanet radial velocity array I: design, commissioning, and early photometric results

    Get PDF
    The MINiature Exoplanet Radial Velocity Array (MINERVA) is a US-based observational facility dedicated to the discovery and characterization of exoplanets around a nearby sample of bright stars. MINERVA employs a robotic array of four 0.7 m telescopes outfitted for both high-resolution spec- troscopy and photometry, and is designed for completely autonomous operation. The primary science program is a dedicated radial velocity survey and the secondary science objective is to obtain high precision transit light curves. The modular design of the facility and the flexibility of our hardware allows for both science programs to be pursued simultaneously, while the robotic control software provides a robust and efficient means to carry out nightly observations. In this article, we describe the design of MINERVA including major hardware components, software, and science goals. The telescopes and photometry cameras are characterized at our test facility on the Caltech campus in Pasadena, CA, and their on-sky performance is validated. New observations from our test facility demonstrate sub-mmag photometric precision of one of our radial velocity survey targets, and we present new transit observations and fits of WASP-52b—a known hot-Jupiter with an inflated radius and misaligned orbit. The process of relocating the MINERVA hardware to its final destination at the Fred Lawrence Whipple Observatory in southern Arizona has begun, and science operations are expected to commence within 2015

    A Korean Predictive Model for Postoperative Nausea and Vomiting

    Get PDF
    Postoperative nausea and vomiting (PONV) is one of the most common and distressing complications after surgery. An identification of risk factors associated with PONV would make it easier to select specific patients for effective antiemetic therapy. We designed a case-controlled study to identify the risk factors for PONV in 5,272 surgical patients. At postoperative 2 and 24 hr, patients were visited and interviewed on the presence and severity of PONV. Thirty nine percent of patients experienced one or more episodes of nausea or vomiting. Five risk factors were highly predictive of PONV: 1) female, 2) history of previous PONV or motion sickness, 3) duration of anesthesia more than 1 hour, 4) non-smoking status, and 5) use of opioid in the form of patient controlled analgesia (PCA), in the order of relevance. The formula to calculate the probability of PONV using the multiple regression analysis was as follows: P (probability of PONV)=1/1+e-Z, Z=-1.885+0.894 (gender)+0.661 (history)+0.584 (duration of anesthesia)+0.196 (smoking status) +0.186 (use of PCA-based opioid) where gender: female=1, male=0; history of previous PONV or motion sickness: yes=1, no=0; duration of anesthesia:more than 1 hr=1, less than or 1 hr=0; smoking status: no=1, yes=0; use of PCA-based opioid: yes=1, no=0

    Analysis of Heme Iron Coordination in DGCR8: The Heme-Binding Component of the Microprocessor Complex

    Get PDF
    DGCR8 is the RNA-binding partner of the nuclease Drosha. Their complex (the “Microprocessor”) is essential for processing of long, primary microRNAs (pri-miRNAs) in the nucleus. Binding of heme to DGCR8 is essential for pri-miRNA processing. On the basis of the split Soret ultraviolet–visible (UV–vis) spectrum of ferric DGCR8, bis-thiolate sulfur (cysteinate, Cys–) heme iron coordination of DGCR8 heme iron was proposed. We have characterized DGCR8 heme ligation using the Δ276 DGCR8 variant and combined electron paramagnetic resonance (EPR), magnetic circular dichroism (MCD), electron nuclear double resonance, resonance Raman, and electronic absorption spectroscopy. These studies indicate DGCR8 bis-Cys heme iron ligation, with conversion from bis-thiolate (Cys–/Cys–) axial coordination in ferric DGCR8 to bis-thiol (CysH/CysH) coordination in ferrous DGCR8. Pri-miRNA binding does not perturb ferric DGCR8’s optical spectrum, consistent with the axial ligand environment being separated from the substrate-binding site. UV–vis absorption spectra of the FeII and FeII–CO forms indicate discrete species exhibiting peaks with absorption coefficients substantially larger than those for ferric DGCR8 and that previously reported for a ferrous form of DGCR8. Electron–nuclear double resonance spectroscopy data exclude histidine or water as axial ligands for ferric DGCR8 and favor bis-thiolate coordination in this form. UV–vis MCD and near-infrared MCD provide data consistent with this conclusion. UV–vis MCD data for ferrous DGCR8 reveal features consistent with bis-thiol heme iron coordination, and resonance Raman data for the ferrous–CO form are consistent with a thiol ligand trans to the CO. These studies support retention of DGCR8 cysteine coordination upon reduction, a conclusion distinct from those of previous studies of a different ferrous DGCR8 isoform
    • 

    corecore