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In Yersinia, the chaperone SycD forms a head-to-head dimer via TPR 1 (helices 1A and 1B), and formation of the dimer could stabilize the interface that may require AscE in the case of AscG.
Recent crystal structure of PcrH showed that it is also a dimer, although the dimer interactions are made through the convex side of the TPR fold instead of the N-terminal region and TPR 1. Also, there are no additional helices N-terminal to TPR 1 in PcrH as the N-terminal 20 residues are disordered and residues 21 31 are unstructured in the crystal structure [17].
The major difference between AcrH (class II chaperone) and AscG (class III chaperone) is that AcrH forms a dimer and contains extra residues at the region N-terminal to the TPR 1 that have the potential to form an additional helix.
IpgC is a class II chaperone of the T3SS in Shigella and each monomer consists of eight helices (H1 H8), with H1 (residues 9 21) situated N-terminal to TPR 1. IpgC forms an asymmetric dimer with H1 of chain A, which is stabilized by a hydrophobic interface provided by H1, H3, H4 and H5 of chain B. H1 and the loop connecting it to H2 show different arrangement in both subunits.
These included representative members from eight different families such as AP2-EREBP (16), AS2 (1), β-helix-loop-helix (2), Homeodomain/HOMEOBOX (2), MYB/HD-like (6), NAC (2), PHD (2), PLATZ (2), TPR (1), and TUB (1).
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Five APC subunits contain TPR domains: CDC27, APC5, CDC16, APC7 and CDC23.
For example, for the target values of FPR =.01 and TPR =.80, the odds ratio equals (TPR × (1-FPR)/ ((1-TPR) × FPR) = 396, as in Table 1.
TPR [16] also builds a word co-occurrence graph.
The catalysts were characterized by XRD, TGA, TPR, H2-chemisorption and BET surface area techniques.
The statistic-based methods, e.g., Wan'07 [32], SC [17], and TPR [16], explore some external text corpus to assist keyphrase extraction.
The catalysts were also characterized by BET surface area, XRD, TPR, NH3-TPD, TEM, XPS and CO chemisorption method.
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