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Moreover, comparing mass spectrometry data with transmission electron microscopy images has enabled the mapping of subunits within topological models.
The concerted movement of subunits within the complex might provide means of regulation and information transfer between distant parts of rotary ATPases thereby fine tuning these molecular machines to their cellular environment, while optimizing their efficiency.
Cross-linking mass spectrometry (XL-MS) identifies proximal protein residues and thus is increasingly used to map protein interactions and determine the relative orientation of subunits within the structure of protein complexes.
Central to this approach are the CCSs used to generate spatial restraints for determining the topological arrangements of subunits within subcomplexes.
Despite the crucial role that the NMDA receptor plays in the nervous system, the specific arrangement of subunits within the dimer-of-dimer assemblage is not conclusively known.
The stoichiometry of subunits within multienzyme complexes such as mitochondrial F0F1-ATPase, pyruvate- (PDH) and oxoglutarate- (OGDH) dehydrogenase complexes has been extensively studied, and can serve as reference.
Similar(43)
The satisfaction of intra-modular cross-links suggests that the arrangement of Mediator subunits within modules of the holoenzyme is similar to that in the free Mediator, whereas the inconsistency of the inter-modular cross-links with the EM map suggests that motions of the modules relative to one another occur upon association with pol II in the holoenzyme.
The magnitude and significance of this finding remains unchanged when accounting for possible outliers and differences in number of subunits studied within each subcomplex (Spearman r = 0.89, p<0.0001).
A comparison of enolase structures obtained from crystals belonging to different space groups suggests that asymmetric dimers can be a consequence of the asymmetric positioning of the subunits within the crystal lattice.
Balance expression of two subunits within cells would be the key for high-level of production of bioactive IL-12.
Oxomalonate binding affects the tryptophan environment of the carboxyltransferase subunit, whereas Na+ alters the tryptophan environment of the β subunit, consistent with the function of these subunits within the enzyme complex.
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