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Tricine SDS-PAGE is Tricine SDS-PAGEectrophoretis systhe for the resolution of preferredsmallelectrophoretic
Experimental results confirm maximum FWHM resolving power in excess of 350,000 at m/z 524 and 600,000 at m/z 195, isotopic resolution of proteins above 40 kDa, and a single-shot dynamic range of 25,000.
Contamination of salts in IEF results in high conductivity, prolonged and poor focusing, electroosmosis, and thus poor resolution of proteins.
Building on our previous work which reported electrophoretic resolution of proteins in 96-plex fsPAG electrophoresis (fsPAGE) assay, we now address an unmet throughput need for riboswitch screening.
Estimation of protein concentration in total homogenates, resolution of proteins by discontinuous, reducing SDS-PAGE, and immunoblot analyses were carried out as described [ 22].
Also, characterization of sub-proteomes like the glycoproteome or phosphoproteome and immunoaffinity depletion of high abundant proteins was attempted in order to reduce complexity and facilitate better resolution of proteins in cervical mucous.
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Relatively low-sensitivity and poor resolution of protein samples require long acquisition times for multidimensional NMR experiments.
Structural biology is a powerful tool for providing a detailed description at atomic resolution of protein functions and suggesting working hypotheses which can then be tested experimentally.
During the last decade of the previous century, progress in the dynamic resolution of protein structure, in the availability of genomic DNA sequence information, and in the synthetic biology of the heterologous production of complex holo-proteins, have brought our understanding of the molecular basis of cellular signal transduction networks down to the atomic level (see e.g. (Ridge et al. 2003)).
Good sensitivity and resolution of protein isoforms could be achieved with this method.
For maximal resolution of protein spots and high loading capacity (330 µg proteins) we used pI 3 11 NL strips (24 cm) for the first dimension.
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