Because it is difficult to determinate the membrane protein's structure by wet-lab experiments, accurate and fast amino acid sequence-based computational methods are highly desired.
For the study of the various non-linear effects generated in ionospheric modulation experiments, accurate calculation of the field intensity variation in the whole reflection region for an electromagnetic wave vertically impinging upon the ionosphere is meaningful.
In numerical experiments, accurate solutions are obtained in constant and smoothly varying media using meshes with only five to six points per wavelength and wave propagation over hundreds of wavelengths.
This demonstrates that the data obtained from this experiment were accurate, precise, and reliable.
This result indicates that not only the experiment is accurate, but also the numerical method for finding the equivalent parameters is reliable.
This is consistent with our experiment on accurate permeability measurement, and can be explained as a result of gas slip flow within such micro pore structure.
Fitting the model to data from the protist experiment yielded accurate predictions of the regional extinction dynamics observed in the system, even with a relatively low level of replication.
Although the results of this experiment were accurate, Fricke misinterpreted the data to mean that the cell membrane is a single molecular layer.
Thereafter, two or more distinctly SILAC-labeled cell populations can be mixed and analyzed in one MS experiment, allowing accurate quantization of proteins from the different cellular states.
To provide reliable confirmation of TPs during laboratory degradation experiment, further accurate MS/MS measurements were performed in order to observe characteristic fragmentation ions of the parent compound.
