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This domain swapping mechanism results in a compact interaction interface.
A compact interaction region (IR), which is the most complicated region in the BEPCII, has been designed to afford a peak luminosity of 1×1033 cm−2 s−1 with an equal beam energy of 1.89 GeV, a cross angle of ±11 mrad, 93 bunches and maximum beam current of 0.91 A.
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Doing so lowers the available degrees of freedom in our representation, resulting in a more compact interaction code less prone to over-fitting.
The TPR domain at the N-terminus consists of three TPR repeats that fold into a compact protein protein interaction moiety.
While the structure of the PleD from P. aeruginosa and the XCC4471GGDEF protein from Xanthomonas campestris showed the presence of compact interaction between the two consecutive, highly conserved glycines in the first two sites, generation of a G to R mutation in Sebox5 has disrupted the compactness which is essential for interaction with the c-di-GMP.
These compact interaction interfaces are typically less than 10 residues in length and are often located within intrinsically disordered regions of highly connected proteins.
In a few minimal group I introns, these tertiary interactions involve direct and compact interactions between RNA domains.
These results fit the predicted compact interactions of -crebanine (1) to Gly2185.42.
And then the G′′ strand forms compact interactions with the E strand in the region BbpThr365 Tyr387 of N2 domain, which "Latch" the ligand binding site and thus stabilize the overall structure.
This means two protomers tightly arranged as a compact dimer (via monomer monomer interactions), which in turn interacts with another compact dimer (via dimer dimer interactions) through long loops leaving a central hole that allows the substrate to enter into the active-site pocket of each subunit.
This inhibiting role implies that PEGylation as well as loading the microspheres with anti-inflammatory drug has a compact effect on the interaction of microspheres with blood proteins.
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