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  • 1990-1994  (5)
  • 1
    Electronic Resource
    Electronic Resource
    Enhanced double-quantum nuclear magnetic resonance in spinning solids at rotational resonance (1992)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 96 (1992), S. 5668-5677 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: The excitation efficiency of double-quantum (2Q) coherences between pairs of spin-1/2 nuclei in rotating powdered solids is greatly enhanced at rotational resonance, where an integer multiple of the spinning speed matches the difference in isotropic chemical shifts. In powdered samples it is possible to transfer up to 50% of the single-quantum magnetization through the 2Q transitions, an order of magnitude more than is achievable in magic-angle-spinning experiments performed off rotational resonance. The effect is simulated numerically by integration of the homogeneous evolution propagator and described analytically using first-order average Hamiltonian theory. Rotational resonance enhanced 2Q filtering is demonstrated experimentally for doubly 13C-labeled samples of zinc acetate and diammonium oxalate monohydrate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.462666
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Double-quantum homonuclear rotary resonance: Efficient dipolar recovery in magic-angle spinning nuclear magnetic resonance (1994)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 101 (1994), S. 1805-1812 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: We describe an efficient method for the recovery of homonuclear dipole–dipole interactions in magic-angle spinning NMR. Double-quantum homonuclear rotary resonance (2Q-HORROR) is established by fulfilling the condition ωr=2ω1, where ωr is the sample rotation frequency and ω1 is the nutation frequency around an applied resonant radio frequency (rf) field. This resonance can be used for double-quantum filtering and measurement of homonuclear dipolar interactions in the presence of magic-angle spinning. The spin dynamics depend only weakly on crystallite orientation allowing good performance for powder samples. Chemical shift effects are suppressed to zeroth order. The method is demonstrated for singly and doubly 13C labeled L-alanine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.467759
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Synthesis and assembly of soybean β-conglycinin in vitro (1992)
    Springer
    Plant molecular biology 18 (1992), S. 259-274 
    Details
    ISSN: 1573-5028
    Keywords: β-conglycinin ; soybean
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The construction of SP6-derived expression plasmids that encode normal and modified β-conglycinin subunits is described. With the exception of an additional methionine at their NH2-terminal ends and the lack of glycans, the normal subunits synthesized at the direction of these plasmids coresponded to mature α and β subunits isolated from soybean seeds. The subunits assembled into trimers in vitro that were equivalent in size to those formed in vivo. This result shows that the glycans are not required either for protein folding or oligomer assembly. Subunits produced from other plasmids, which had modifications in a highly conserved hydrophobic region in the COOH-terminal end of the subunits, either did not assemble or assembled at an extremely low rate compared to unmodified subunits. Structural changes at the more hydrophilic NH2-terminal end had mixed effects. Several subunits modified in this region assembled into trimers at rates that were either equal or greater than those for normal α subunits. Others assembled less completely than the normal subunits. Our results indicate that the in vitro synthesis and assembly assay will be useful in evaluating structure-function relationships in modified β-conglycinin subunits. The results also show that structural changes at the NH2-terminal end of the subunits are tolerated to a greater extent than modifications in the hydrophobic conserved region in the COOH-terminal half of the subunits, and this information will be useful in efforts to improve soybean quality.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00034954
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Characterization of soybean vegetative storage proteins and genes (1990)
    Springer
    Theoretical and applied genetics 79 (1990), S. 785-792 
    Details
    ISSN: 1432-2242
    Keywords: Vegetative storage protein ; Nitrogen ; Soybean ; Glycine max
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Soybean vegetative storage proteins (VSPs) were purified and characterized. Anion exchange HPLC resolved partially purified VSPs into fractions containing 27-kD/27-kD and 29-kD/29-kD homodimers and 27-kD/29-kD heterodimers. Reversed-phase HPLC resolved partially purified VSPs into three fractions. One fraction contained only 27-kD VSP and the other two contained 29-kD VSP. The two 29-kD VSP fractions differed with respect to their cyanogen bromide cleavage patterns, an observation that indicated the 29-kD VSPs were heterogeneous. Genomic clones that contained 29-kD VSP genes were also isolated and characterized. One genomic clone contained a complete 29-kD VSP gene and was sequenced. The coding region in the clone contained two introns whose borders had regulatory sequences typical of other eukaryotic genes. Putative polyadenlyation signals were present in the 3′-flanking region of the gene, while putative TATA, CAAT, and enhancer core sequences were found in the 5′-flanking regions. A second genomic clone that was studied contained the 5′ regions of two partial 29-kD VSP genes in an inverted linkage. Genomic DNA gel blots showed that the two genes were organized in the same arrangement in the soybean genome.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00224246
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Genetic mapping of the Gy4 and Gy5 glycinin genes in soybean and the analysis of a variant of Gy4 (1994)
    Springer
    Theoretical and applied genetics 89 (1994), S. 297-304 
    Details
    ISSN: 1432-2242
    Keywords: Storage protein ; Genome ; RFLP
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The predominant storage protein of soybean [Glycine max (L.) Merr.] seed is a globulin called glycinin. Thus far five genes encoding glycinin subunits have been described, and these are denoted by the gene symbols Gy1 to Gy5. The objectives of this study were to map two of these genes, Gy4 and Gy5, and to conduct a genetic analysis of a subunit size-variant from an allele of Gy4. For this purpose a population was formed with an interspecific cross between PI 468916 (G. soja) and A81-356022 (G. max). The two size forms of G4, the subunit from Gy4, segregated codominantly in the mapping population, and were due to a short insertion in the hypervariable region of the mutant protein. The biochemical and molecular characteristics of the two subunits indicate that they are produced from alternate alleles of the same gene. The gene symbols Gy a and Gy b have been assigned to the normal and variant genes, respectively. When genomic DNA from the two parents was probed with a Gy4 cDNA, RFLPs were identified for both Gy4 and Gy5. Using these genetic markers, the Gy4 and Gy5 glycinin genes were mapped in linkage group “O” and “F” on the public soybean genomic map.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00225158
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    Paper (German National Licenses)
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