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In this paper, we focus on two examples of wave trains in a loop segment and the main statistical parameters in their wavelet power and global spectra are studied and discussed.
The X-ray crystal structure of the reaction product of acetylcholinesterase (AChE) with the inhibitor diisopropylphosphorofluoridate (DFP) showed significant structural displacement in a loop segment of residues 287 290.
Consequently, we found that even for a small and relatively rigid protein, engineering a loop segment enables to alter conformational dynamics through a long-range effect, preserving the native-state structure and important aspects of function.
There is no contact between the start and end residues of a loop segment u.
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17, 18 MSK1 contains two kinase domains separated by a flexible loop segment.
When the mismatch strain exceeds the generation limit, which is particle size dependent, the generation of dislocations lowers the system energy, and a stable dislocation loop segment will be generated and bulge out from the particle matrix interface.
An ∼85 Å long α-helix (αT) extends from the post of the FH2 domain, and the autoregulatory DAD domain segment is connected to the end of helix αT by a 10-residue loop segment.
The only enzyme substrate complex in which a disordered L2 loop segment is observed is I243N Y306F HDAcomplexedxed with the tetrapeptide assay substrate (PDB accession code 4QA3): in monomer B only, D88 and D89 are disordered and accordingly not modeled.
Only T288 of monomer II (proposed as the substrate molecule above) with a more flexible activation loop segment can be rearranged at a close distance to the γ-phosphate of AMPPCP without displacing the AMPPCP from its original position.
In agreement with the prediction of a simple statistical mechanical model for β-hairpin formation, our results show that the separation between the loop segment and an interstrand cluster of hydrophobic side-chains strongly influences β-hairpin size and stability, with a smaller separation leading to greater stability.
Both kinases are activated by phosphorylation on a threonine residue within the activation loop segment of the catalytic subunit.
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