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Interaction networks between the terminal saccharides of HBGAs and the amino acids forming the binding interfaces have been thoroughly described [reviewed in (Tan and Jiang, 2014, 2011, 2010)].
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(A) Phylogenic tree of the nine known GI genotypes with indications of Norwalk virus (GI.1), FUV258 (GI.2), TCH060 (GI.7), and Boxer virus (GI.8) whose crystal structures of the HBGA-binding interfaces have been determined.
The technique has played a dominant role in forming the field of synthetic binding protein engineering, where novel interfaces have been generated from libraries built using antibody fragment frameworks and also alternative scaffolds.
The DNA binding and dimerization interface have been solved by high resolution X-ray crystallography in the apo- and DNA-bound forms [13], [14].
In particular, the long-held belief that agonist binding sites are formed only at α interfaces has been challenged by increasing evidence for a viable agonist binding site at α interfaces.
The influence on binding of disordered regions outside the interacting interface has been theoretically predicted [32] and experimentally observed before [33].
The extent of lipase binding is related to the physicochemical as well as the compositional structure of the interface, for which the expression "quality of the interface" has been coined 10.
A graphical user interface has been implemented.
The database interface has been designed to be user-friendly graphic user interface.
Last but not least, DARPins have a relatively large binding interface and have been engineered, mostly via phage display and ribosome display, to bind a wide range of targets with pmol/L nmol/L affinities (Pluckthun, 2015).
The exquisite side chain close-packing in the protein core and at binding interfaces has prompted a conviction that packing selectivity is the primary mechanism for molecular recognition in folding and/or binding reactions.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com