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Past efforts to design repeat protein-based molecular recognition tools have focused on the creation of templates from the consensus of individual repeats, regardless of their natural context.
Aptamers are useful molecular recognition tools in research, diagnostics, and therapy.
Biomarker discovery and specific molecular recognition tools may unravel the interrelationships amongst Aβ assemblies and facilitate detection and characterization of these assemblies early in the course of AD.
In the past two decades, an alternative class of molecular recognition tools, aptamers, has emerged offering important advantages relative to antibodies, including rapid selection in vitro, high stability under non-physiologic conditions, straightforward chemical manipulation, low immunogenicity, and cost-effectiveness [18], [19].
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Owing to its diversified structures, high affinity, and specificity for binding a wide range of non-nucleic acid targets, aptamer is a useful molecular recognition tool for the design of various biosensors.
Molecular recognition is also a useful tool for lesion detection.
Though similar to the more familiar hydrogen bonding, four primary differences between these two interactions make halogen bonding a unique tool for molecular recognition and the design of functional materials.
The molecular recognition property makes them a versatile tool for complexation of organic and biomolecules.
We here present a new type of repeat proteins, the αRep proteins, as a tool for specific molecular recognition of protein targets inside living cells.
By a mechanism of molecular recognition, the MIPs are used as selective tools for the development of various analytical techniques such as liquid chromatography, capillary electrochromatography, solid-phase extraction (SPE), binding assays and biosensors.
Apart from the intrinsic academic interest in characterizing the determinants of molecular recognition, the scientific community increasingly requires computational tools to model the physiological interactions in which a protein is involved, once its 3-D structure has been solved.
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