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Loop 1 (residues 117 131), Loop 2 (residues 192 201) and the substrate recognition peptide (residues 94 102) of PolB exhibit considerable conformational flexibility and adopt distinct structures upon binding to different substrate analogs.
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Proteins with long-disorder regions have unique biophysical traits that enable the binding to different substrates, often at different cellular conditions (Wright and Dyson, 2009).
Variants in TpLRR could also lead to different functions altogether (such as binding to different substrates), and possibly contribute to rapid adaptations to environmental changes (as for example between the male and female urogential tracts or between the various mucosal landmarks) as known, or suggested, for different parasitic and other microbial eukaryotes [ 43, 44, 71, 72].
Each integrin dimer binds to different substrates; however, binding may be redundant among dimers.
Further clarification of the role of the TIR homologs (AFB1, AFB2, and AFB3) has come from a recent study which reported that the function of the different TIR/AFB proteins in the auxin response could be attributed to their relative expression, which is under the control of post-transcriptional regulation, or related to their binding to different Aux/IAA substrates [13].
Fluorescence anisotropy was used to measure equilibrium dissociation constants defining PrimPol binding to different p/t-DNA substrates (Table 1).
Thus, interference can be low if two compounds bind to different sites of the substrate binding site [ 31].
The two PP1Y monooxygenases (Additional file 1: Figure S5) mainly differ in the substrate-binding region, possibly to allow different substrate specificity.
(1202) Extensive photoaffinity labeling studies on binding of different substrates to PGP and single-point mutagenesis analyses, as recently reviewed, 1045) delineate the associations between structure and function.
However, ultra-affinity was implicitely suggested in a series of works assessing the binding of different substrates to Hsp70s, always in the presence of a co-localized JDP, thus ensuring maximal hydrolysis acceleration upon substrate binding (Misselwitz et al., 1998; Laufen et al., 1999; Sullivan et al., 2001).
We observed that some of the regions of the protein structure that exhibit such fluctuations coincide with the protein's binding surfaces with different substrate like GTPase effector domain (GED) of dynamin, SUMO binding motifs (SBM), E1 (activating enzyme, SAE1/SAE2) and E2 (conjugating enzyme, UBC9) enzymes of sumoylation machinery, reported earlier.
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