Seed production of barnyardgrass (Echinochloa crus-galli) in response to time of emergence in cotton and rice

The spread of herbicide resistance in barnyardgrass (Echinochloa crus-galli (L.) Beauv.) poses a serious threat to crop production in the southern United States. A thorough knowledge of the biology of barnyardgrass is fundamental for designing effective resistance-management programmes. In the present study, seed production of barnyardgrass in response to time of emergence was investigated in cotton and rice, respectively, in Fayetteville and Rohwer, Arkansas, over a 2-year period (2008–09). Barnyardgrass seed production was greater when seedlings emerged with the crop, but some seed production was observed even if seedlings emerged several weeks after crop emergence. Moreover, barnyardgrass seed production was highly variable across environments. When emerging with the crop (0 weeks after crop emergence (WAE)), barnyardgrass produced c. 35 500 and 16 500 seeds/plant in cotton, and c. 39 000 and 2900 seeds/plant in rice, in 2008 and 2009, respectively. Seed production was observed when seedlings emerged up to 5 WAE (2008) or 7 WAE (2009) in cotton and up to 5 WAE (2008, 2009) in rice; corresponding seed production was c. 2500 and 1500 seeds/plant in cotton, and c. 14 700 and 110 seeds/plant in rice, in 2008 and 2009, respectively. The results suggest that cultural approaches that delay the emergence of barnyardgrass or approaches that make the associated crop more competitive will be useful in integrated management programmes. In the context of herbicide resistance management, it may be valuable to prevent seed return to the seedbank, irrespective of cohorts. The findings are vital for parameterizing herbicide resistance simulation models for barnyardgrass

Capture Velocity for a Magneto-Optical Trap in a Broad Range of Light Intensity

In a recent paper, we have used the dark-spot Zeeman tuned slowing technique [Phys. Rev. A 62, 013404-1, (2000)] to measure the capture velocity as a function of laser intensity for a sodium magneto optical trap. Due to technical limitation we explored only the low light intensity regime, from 0 to 27 mW/cm^2. Now we complement that work measuring the capture velocity in a broader range of light intensities (from 0 to 400 mW/cm^2). New features, observed in this range, are important to understant the escape velocity behavior, which has been intensively used in the interpretation of cold collisions. In particular, we show in this brief report that the capture velocity has a maximum as function of the trap laser intensity, which would imply a minimum in the trap loss rates.Comment: 2 pages, 2 figure

Loading of a Rb magneto-optic trap from a getter source

We study the properties of a Rb magneto-optic trap loaded from a commercial getter source which provides a large flux of atoms for the trap along with the capability of rapid turn-off necessary for obtaining long trap lifetimes. We have studied the trap loading at two different values of background pressure to determine the cross-section for Rb--N$_2$ collisions to be 3.5(4)x10^{-14} cm^2 and that for Rb--Rb collisions to be of order 3x10^{-13} cm^2. At a background pressure of 1.3x10^{-9} torr, we load more than 10^8 atoms into the trap with a time constant of 3.3 s. The 1/e lifetime of trapped atoms is 13 s limited only by background collisions.Comment: 5 pages, 5 figure

Alumina and Synthesis Intermediates Derived from Diethylkaluminum Amide, Benzaldehyde and Water

The reaction of diethylaluminum amide [Et2AINH2] with benzaldehyde in toluene produces a solution of ethylaluminoxane polymer [EtAlO] and hydrobenzamide [PhCH=NCH(Ph)N=CHPh]. Alumina then is precipitated by the addition of water. Transition aluminas that may be useful in heterogeneous catalyst applications are obtained after calcining. Details of the chemistry of solution intermediates according to 1H NMR and the properties of the alumina product according to surface area analyses and powder x-ray diffraction are described

Ohio Economic Insects and Related Anthropods

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Sensitivity-Enhanced NMR Reveals Alterations in Protein Structure by Cellular Milieus

Biological processes occur in complex environments containing a myriad of potential interactors. Unfortunately, limitations on the sensitivity of biophysical techniques normally restrict structural investigations to purified systems, at concentrations that are orders of magnitude above endogenous levels. Dynamic nuclear polarization (DNP) can dramatically enhance the sensitivity of nuclear magnetic resonance (NMR) spectroscopy and enable structural studies in biologically complex environments. Here, we applied DNP NMR to investigate the structure of a protein containing both an environmentally sensitive folding pathway and an intrinsically disordered region, the yeast prion protein Sup35. We added an exogenously prepared isotopically labeled protein to deuterated lysates, rendering the biological environment “invisible” and enabling highly efficient polarization transfer for DNP. In this environment, structural changes occurred in a region known to influence biological activity but intrinsically disordered in purified samples. Thus, DNP makes structural studies of proteins at endogenous levels in biological contexts possible, and such contexts can influence protein structure.United States. National Institutes of Health (GM-025874)United States. National Institutes of Health (EB-003151)United States. National Institutes of Health (EB-002804)United States. National Institutes of Health (EB-002026

Combining DNP NMR with segmental and specific labeling to study a yeast prion protein strain that is not parallel in-register

The yeast prion protein Sup35NM is a self-propagating amyloid. Despite intense study, there is no consensus on the organization of monomers within Sup35NM fibrils. Some studies point to a â-helical arrangement, whereas others suggest a parallel inregister organization. Intermolecular contacts are often determined by experiments that probe long-range heteronuclear contacts for fibrils templated from a 1:1 mixture of 13 C- and 15 N-labeled monomers. However, for Sup35NM, like many large proteins, chemical shift degeneracy limits the usefulness of this approach. Segmental and specific isotopic labeling reduce degeneracy, but experiments to measure long-range interactions are often too insensitive. To limit degeneracy and increase experimental sensitivity, we combined specific and segmental isotopic labeling schemes with dynamic nuclear polarization (DNP) NMR. Using this combination, we examined an amyloid form of Sup35NM that does not have a parallel in-register structure. The combination of a small number of specific labels with DNP NMR enables determination of architectural information about polymeric protein systems. Keyword: [PSI+] prion; solid-state NMR; amyloid; Sup35; dynamic nuclear polarizationNational Institutes of Health (U.S.) (Grants GM-025874)National Institutes of Health (U.S.) (Grants EB-003151)National Institutes of Health (U.S.) (Grants EB-002804)National Institutes of Health (U.S.) (Grants EB-002026

Thermodynamics of Heat Shock Response

Production of heat shock proteins are induced when a living cell is exposed to a rise in temperature. The heat shock response of protein DnaK synthesis in E.coli for temperature shifts from temperature T to T plus 7 degrees, respectively to T minus 7 degrees is measured as function of the initial temperature T. We observe a reversed heat shock at low T. The magnitude of the shock increases when one increase the distance to the temperature $T_0 \approx 23^o$, thereby mimicking the non monotous stability of proteins at low temperature. Further we found that the variation of the heat shock with T quantitatively follows the thermodynamic stability of proteins with temperature. This suggest that stability related to hot as well as cold unfolding of proteins is directly implemented in the biological control of protein folding. We demonstrate that such an implementation is possible in a minimalistic chemical network.Comment: To be published in Physical Review Letter