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Sökning: WFRF:(Wildes David)

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1.
  • Jacobsen, Henrik, et al. (författare)
  • Spin dynamics of the director state in frustrated hyperkagome systems
  • 2021
  • Ingår i: Physical Review B. - : American Physical Society. - 2469-9969 .- 2469-9950. ; 104:5
  • Tidskriftsartikel (refereegranskat)abstract
    • We present an experimental study of the magnetic structure and dynamics of two frustrated hyperkagome compounds, Gd3Ga5O12 and Gd3Al5O12. It has previously been shown that Gd3Ga5O12 exhibits long-range correlations of multipolar directors that are formed from antiferromagnetic spins on loops of ten ions. Using neutron diffraction and reverse Monte Carlo simulations we prove the existence of similar magnetic correlations in Gd3Al5O12, showing the ubiquity of these complex structures in frustrated hyperkagome materials. Using inelastic neutron scattering we shed further light on the director state and the associated low-lying magnetic excitations. In addition, we have measured quasielastic dynamics that show evidence of spin diffusion. Finally, we present AC susceptibility measurements on both Gd3Ga5O12 and Gd3Al5O12, revealing a large difference in the low-frequency dynamics between the two otherwise similar compounds.
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2.
  • Maxwell, Karen L., et al. (författare)
  • Protein folding : Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins
  • 2005
  • Ingår i: Protein Science. - : Wiley. - 0961-8368 .- 1469-896X. ; 14, s. 602-16
  • Tidskriftsartikel (refereegranskat)abstract
    • Recent years have seen the publication of both empirical and theoretical relationships predicting the rates with which proteins fold. Our ability to test and refine these relationships has been limited, however, by a variety of difficulties associated with the comparison of folding and unfolding rates, thermodynamics, and structure across diverse sets of proteins. These difficulties include the wide, potentially confounding range of experimental conditions and methods employed to date and the difficulty of obtaining correct and complete sequence and structural details for the characterized constructs. The lack of a single approach to data analysis and error estimation, or even of a common set of units and reporting standards, further hinders comparative studies of folding. In an effort to overcome these problems, we define here a "consensus" set of experimental conditions (25°C at pH 7.0, 50 mM buffer), data analysis methods, and data reporting standards that we hope will provide a benchmark for experimental studies. We take the first step in this initiative by describing the folding kinetics of 30 apparently two-state proteins or protein domains under the consensus conditions. The goal of our efforts is to set uniform standards for the experimental community and to initiate an accumulating, self-consistent data set that will aid ongoing efforts to understand the folding process.
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