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Alternatively, the inorganic phosphate may occupy binding pockets that are normally occupied by the phosphate moieties of NADP+ during catalysis, thereby stabilizing the enzyme.
Comparison of these structures with the CKI-7-bound casein kinase 1 reveals features in the binding pockets that are distinct in the bacterial kinases and could be exploited for the design of a bacterial kinase specific inhibitor.
Most notably, there are seven riboswitch families with four distinct binding pockets that are specific for SAM and/or S-adenosylhomocysteine (SAH) although it is not clear whether they share common ancestries [ 2].
If dynamin 1 also forms the GTPase domain homodimer as observed for BDLP and GBP1, this arrangement results in nucleotide binding pockets that are essentially closed to the external environment and suggests against a direct catalytic or RGS-type allosteric (Narayanan et al., 2005) involvement of the GED.
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Despite the retention of the multisite binding mechanism in the mutants, functional manifestations reveal an exquisite sensitivity to even minor structural changes in the binding pocket that are introduced by conservative substitutions such as I369F, I369L, and A370V.
However, Brown and collaborators have subsequently shown that these sites are involved in peptide-binding pockets that are crucial for peptide capture (Stern et al. 1994).
Their antigen-recognition sites typically form a convex surface with a large CDR (complementarity-determining region) loop 3 (capableapable of reaching antigen-binding pockets that are less antigenic for other types of binders.
A binding pocket that is likely to bind a ligand will have an Sscore greater than 0.8 and a Dscore greater than 0.83 [44] 44].
Consequently, they form a characteristic "glove" shape, encompassing a hydrophobic binding pocket that is able to bind specific small organic molecules [4].
One obvious common feature of these two groups of GT41 proteins is that both bind sugars donors that are activated by UDP, requiring a binding pocket that is formed by the C-terminal half of the GT-B domain (Fig. 1A) [18], [18].
The relatively smaller OPR3 residues allow formation of a wider substrate binding pocket that is less enantio-restrictive.
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