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Ultimately, simultaneous detection of HSA and hCRP model proteins was demonstrated on UCNPs-encoded multicolor microbeads via sandwich assay in this proof-of-concept study.
We used a minimalist on-lattice model to analyze how the dynamics of the reassembly process for two model proteins was affected by the location of the split site.
The total level of all other model proteins was constant.
The expression of both model proteins was controlled by the constitutive glyceraldehyde-3-phosphate dehydrogenase (GAP) promoter of P. pastoris.
To confirm that product ion spectra were acquired at ideal conditions for UVPD, a series of model proteins was infused to allow assessment and optimization of experimental parameters to be used in an online LC MS method.
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Advanced refolding strategies by pulsed refolding and temperature leap, favoring the native pathway of specific model proteins were also implemented.
Various model proteins were efficiently entrapped on/into the nanoparticles under different conditions: encapsulation, covalent immobilization, and physical adsorption.
Three model proteins were resolved in an EFGF channel of this design.
In order to investigate this novel delivery system, formulations containing IFN-β-1a asd trypsinogen as model proteins were developed.
The relative metastabilities of the model proteins were calculated as a function of temperature, pressure and chemical activities or fugacities of basis species.
Two model proteins were used for the construction of chimeras, a lipase from Bacillus pumilus (BplA) and the enhanced green fluorescent protein (EGFP).
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