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There are four major mechanisms for the modification of the structures of multi-subunit complexes: (1) recruitment of entirely new proteins; (2) paralog exchange; (3) alternative splice variants; and (4) modification of existing proteins (such as phosphorylation).
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Furthermore, modification of the structure is focused on improving the SRS in the QC-RL.
In some cases, we can even identify how modification of the structure impacts the property of interest.
The optical transitions are thoroughly examined to reveal the impact of subtituents on both absorption and fluorescence, mainly through the modification of the structure in the excited state.
Scanning electron microscope (SEM) showed some modification of the structure with a slight destruction of cell walls after DIC treatment.
Raman spectroscopy of similar mixtures has shown that ion irradiation causes a modification of the structure of the samples which evolve towards an amorphous carbon.
Here we advocate the third approach, modification of the structure of the lubricant film; this approach leads to what we call composite-film bearings (CFB).
It is difficult to detect the formation of Cd complexes or modification of the structure of HAP by Cd due to the similar ionic radii of Ca (0.99 Å) and Cd (0.97 Å).
The convergence of the algorithm is analyzed in both the dynamic process phase and the phase following the modification of the structure.
Systematic modification of the structure of the photoreagent provides valuable information on the binding site recognition as well as the mechanism of the photocleavage reaction.
CBM is for modification of the structure of the current CPN model while CBC is for the composition of another CPN into the current CPN.
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