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The X-ray structure of the N-terminal 24 kDa ParE, responsible for ATP binding has been solved.
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The three-dimensional structures of domains associated with substrate adenylation and covalent binding have been solved as well as the structure of a priming enzyme required for the post-translational modification of NRPS.
The three-dimensional structure of numerous receptor binding proteins of tailed phages has been solved.
To understand the receptor ligand cross-talk, the NMR structure of CR56 has been solved and ligand binding experiments with RAP domain 1 (RAPd1) have been performed.
The BbCRASP-1 protein is the first bacterial factor H/FHL-1-binding protein for which the atomic structure has been solved.
Glutamine-binding protein (GlnBP) is one of the periplastic binding proteins from Gram-negative bacteria, whose crystal structure has been solved in both open and closed forms.
The crystal structure of IRP1 has been solved in both the c-aconitase-binding [ 136] and IRE-binding [ 137] forms, although the structure of IRP2 has not yet been determined.
The crystal structure of R-Spondin binding to the ectodomains of LGR5, RNF43 and ZNRF3 has been solved recently [ 64, 65].
The crystal structure of the HIN domain has been solved, and it displays two oligonucleotide/oligosaccharide-binding (OB) folds forming the DNA-binding surface (Jin et al. 2012).
Glutamine-binding protein (GlnBP) is one such protein, whose crystal structure has been solved in both open and closed forms.
The crystal structure for GtfB has been solved and provides insights into the sugar and aglycone substrate binding sites, creating possibilities for remodeling the protein for different sugar or substrate binding.
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