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The origin of ΔχDIA was attributed to preferential orientation of bond direction with respect to a magnetic principle axis of crystal (Uyeda, 2004a).
At the same time, fraction of adsorbed segment fa and average orientation of bond 〈P2(cos θ)〉 are also investigated.
Residual dipolar couplings (RDC) measured for samples weakly aligned in dilute liquid crystalline media, such as phage pf1 [15], [15], are directly related to the orientation of bond vectors to the axes of the alignment tensor [16].
Residual dipolar couplings (RDCs) are determined in partially aligned media and give direct information about the orientation of bond vectors relative to the molecular alignment tensor.
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At a high level, the residual dipolar coupling data used in NVR is global, giving orientations of bond vectors with respect to a coordinate frame, whereas the NOESY data used here is local, giving distances only between close protons.
For a folded protein, the magnitude and sign of the residual dipolar couplings depend on the orientation of each bond vector relative to the alignment tensor of the entire molecule, which reorients as a single entity.
This 'inline' orientation of phosphodiester bond is not possible in dsRNA, which adopts helical secondary structure [9].
NMR RDCs contain information about the orientation of atomic bond vectors in a protein and thus can be used to test the validity of a particular structural model (36).
In the isoprenoid alcohol menthol, for example, three of the hydrogen atoms of cyclohexane have been replaced, each by a different group; the structures shown here specify the orientation of the bonds and the conformation of the ring in the natural form of menthol.
Three types of specimen were considered, which differ for the fibres orientation of the bonded surfaces.
Thus, at the moment of instability under tension in armchair direction, the orientation of atomic bonds is characterized by angles of 130° and 130°, while for tension in zigzag direction, they are 114° and 132°, respectively (Fig. 3).
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