63 research outputs found
Laser-induced splittings in the nuclear magnetic resonance spectra of the rare gases
Circularly polarized laser field causes a shift in the nuclear magnetic
resonance (NMR) spectra of all substances. The shift is proportional to the
intensity of the laser beam and yields oppositely signed values for left- and
right-circularly polarized light, CPL -/+, respectively. Rapid switching -- in
the NMR time scale -- between CPL+ and CPL- gives rise to a splitting of the
NMR resonance lines. We present uncorrelated and correlated quadratic response
calculations of the splitting per unit of beam intensity in the NMR spectra of
Ne, Kr, and Xe. We study both the regions far away from
and near to optical resonance and predict off-resonance shifts of the order
0.01, 0.1, and Hz for Ne, Kr, and Xe,
respectively, for a beam intensity of 10 W/cm. Enhancement by several
orders of magnitude is predicted as the beam frequency approaches resonance.
Only then can the effect on guest Xe atoms be potentially useful as a
probe of the properties of the host material.Comment: 5 pages, 1 figur
Sequential decoupling of negative-energy states in Douglas-Kroll-Hess theory
Here, we review the historical development, current status, and prospects of
Douglas--Kroll--Hess theory as a quantum chemical relativistic electrons-only
theory.Comment: 15 page
Blind testing cross-linking/mass spectrometry under the auspices of the 11th critical assessment of methods of protein structure prediction (CASP11)
Determining the structure of a protein by any method requires various contributions from experimental and computational sides. In a recent study, high-density cross-linking/mass spectrometry (HD-CLMS) data in combination with ab initio structure prediction determined the structure of human serum albumin (HSA) domains, with an RMSD to X-ray structure of up to 2.5 Å, or 3.4 Å in the context of blood serum. This paper reports the blind test on the readiness of this technology through the help of Critical Assessment of protein Structure Prediction (CASP). We identified between 201-381 unique residue pairs at an estimated 5% FDR (at link level albeit with missing site assignment precision evaluation), for four target proteins. HD-CLMS proved reliable once crystal structures were released. However, improvements in structure prediction using cross-link data were slight. We identified two reasons for this. Spread of cross-links along the protein sequence and the tightness of the spatial constraints must be improved. However, for the selected targets even ideal contact data derived from crystal structures did not allow modellers to arrive at the observed structure. Consequently, the progress of HD-CLMS in conjunction with computational modeling methods as a structure determination method, depends on advances on both arms of this hybrid approach
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