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The Hsp70/Hsp110 complex constitutes a small fraction of the total Hsp70; however, it is an "active" complex in the sense that it is involved in active chaperoning of client proteins.
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Taken together, these results suggest that differential phosphorylation of Cos2 may regulate the formation of distinct Smo-Cos2-Fu complexes: Ser572 phosphorylation disrupts the inactive complex in which Cos2 binds to the membrane proximal region of Smo C-tail, whereas Ser931 phosphorylation favors the formation of an active complex in which Cos2 binds to the C-terminal region of Smo.
Confirming propeptide specificity for GGCX-nanodiscs and extended stability of the protein complex affirmed that the conformational information derived from deuterium labeling was highly reflective of the active complex in vivo.
Oxalic acids behave as photo-active complexes in the presence of ferric ions at acidic pH, which undergo photo-decarboxylation reaction (Equation 5) [18] 18]: Fe III RCO 2 2 + + hυ → Fe 2 + + CO 2 + R · Open image in new window (5).
We use stochastic transitions, with a relative rate of 100/a.u. for the formation of transcriptionally active complex, so in the case of a realistic system with multiple genes, the genes are fired asynchronously and multiple trajectories with different sequences of gene activation are sampled.
D-type cyclins associate with cyclin-dependent kinases to form active complexes involved in the regulation of the retinoblastoma protein, and thus are involved in cell-cycle regulation.
However, the promising one-step synthesis of complexing composite materials, which leads to even distribution of active complexing groups in the polymer immobilized on the surface of the inorganic matrix, is direct (in situ) formation of the polymer layer in the presence of particles of inorganic matrix [10 12].
(D ) Allosteric activity regulation is achieved by interconversion between an active α2β2 complex in the presence of the allosteric activity effector ATP and an inactive α4β4 species when dATP binds to the allosteric activity site (PDB ID: 3UUS).
The Ruiz-Tolima Volcanic Massif (RTVM) is an active volcanic complex in the Northern Andes, and understanding its geological structure is critical for hazard mitigation and guiding future geothermal exploration.
Our data show that in the active complex, the catalytic domains from two resolvase dimers form a central core, while the DNA binding domains and the DNA lie on the outside.
Even though Hamartin and Tuberin (TSC1 and TSC2) exist and are active as a complex in the regulation of the mTOR pathway, our data show that the RapGAP homologous domain in TSC2 apparently contains the full catalytic machinery.
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