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  • Céolin, Denis, et al. (författare)
  • Recoil-induced ultrafast molecular rotation probed by dynamical rotational Doppler effect
  • Annan publikation (övrigt vetenskapligt/konstnärligt)abstract
    • Observing and controlling molecular motion, and in particular rotation,is a fundamental topic in physics and chemistry. In order toinitiate ultrafast rotation, one needs a way to transfer a large angularmomentum to the molecule. As a showcase, this was performedby hard x-ray C1s ionization of carbon monoxide, accompanied byspinning-up the molecule via the recoil “kick” of the emitted fast photoelectron.To visualize this molecular motion, we use the dynamicalrotational Doppler effect and an X-ray “pump-probe” device offeredby nature itself: the recoil-induced ultrafast rotation is probed by subsequentAuger electron emission. The time information in our experimentorigins from the natural delay between the C1s photoionizationinitiating the rotation and the ejection of the Auger electron. From amore general point of view, time-resolved measurements can be performedin two ways: either to vary the "delay" time as in conventionaltime-resolved pump-probe spectroscopy and to use the dynamicsgiven by the system, or to keep constant "delay" time and to manipulatethe dynamics. Since in our experiment we cannot change the delaytime given by the core-hole lifetime $\tau$, we use the second optionand control the rotational speed by changing the kinetic energy of thephotoelectron. The recoil-induced rotational dynamics controlled insuch a way is observed as a photon-energy dependent asymmetryof the Auger lineshape, in full agreement with theory. This asymmetryis explained by a significant change of the molecular orientationduring the core-hole lifetime, which is comparable with the rotationalperiod.
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  • Harczuk, Ignat, 1987-, et al. (författare)
  • First hyperpolarizability of collagen using the point dipole approximation
  • Annan publikation (övrigt vetenskapligt/konstnärligt)abstract
    • The application of localized hyperpolarizabilities to predict a total protein hyperpolariz-ability is presented for the first time, using rat-tail collagen as a demonstration example. Weemploy a model comprising the quadratic Applequist point-dipole approach, the so-calledLoProp transformation and a procedure with molecular fractionation using conjugate capsin order to determine the atomic and bond contributions to the net β tensor of the collagen[(PPG)3 ]10 triple-helix. By using Tholes exponential damping modification to the dyadic ten-sor in the Applequist equations, a correct qualitative agreement with experiment is found. Theintensity of the βHRS signal and the depolarization ratios are best reproduced by decomposingthe LoProp properties into the atomic positions, and using Tholes exponential damping withthe original damping parameter. Some ramifications of the model for general protein propertyoptimization are briefly discussed.
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