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Consistently, immunohistochemistry detected very weak protein signals in the cytoplasms of cardiomyocytes at the failing stage, but myocytes nuclei were heavily labeled.
This approach does not require preservation of protein complexes in vitro, making it an ideal approach to identify transient or weak protein complexes.
Both alternative and constitutive exons are recognized by multiple weak protein:RNA interactions and different exons differ in the interactions which are determinative for exon usage.
The presence of both PARPSso and DNA in the organic phase, which corresponds a weak protein pattern to (data not shown), suggests a very tight association of DNA and enzyme with apolar molecules (perhaps membrane lipids?).
Recent methodological developments have helped characterize weak protein interactions, and have in particular been applied to the study of proteins that are mostly unfolded alone but form well-defined complexes upon interaction.
The microstructure examined by confocal laser scanning microscopy (CLSM) was only slightly affected by the concentrations of inulin in the range studied, possibly due to weak protein interactions between the inulin and the milk protein network.
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The proteins inside membrane nanoclusters are restrained only by weak intermolecular protein:protein and protein:lipid interactions [15,16].
Most of these signals belong to non-coding ones, considering their weak protein-coding potential.
Tup1-Ssn6 recruitment and corresponding complex formation occurs by relatively weak protein-protein interactions with either Tup1 or Ssn6 [18].
Lack of direct interaction between SNF and SXL was also revealed by our NMR chemical shift perturbation experiment, which can detect extremely weak protein-protein interactions (Kd>10−4 M) [38].
Immunofluorescent staining has been used in these transfection experiments to show that weak protein-protein interactions between the cytoplasmic domains of highly abundant ER imbedded proteins are sufficient to induce membrane stacking and whorl formation.
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