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In recent years, the elucidation of the structures of many signalling molecules has allowed new insights into the molecular mechanisms that govern signal transduction events.
This development has paved the way for further controlled polymerisations, and, by understanding the reaction mechanism of guest molecules, has allowed for the design of new frameworks for molecular confinement, alignment and conversion.
The fine-mapping of epitopes, typically 9 amino acid (AA) long but ranging from 8 to 11 AA, together with data on their binding properties to HLA molecules, has allowed definition of HLA class I allele-specific sequence motifs that are able to prime virus-specific CD8+ T-cell responses.
Detecting changes in the salivary concentrations of these molecules has allowed the detection of oral and systemic diseases.
Besides using imaging to measure plasticity, the development of fluorescent sensors for signalling molecules has allowed scientists to directly measure signalling activity.
The ability to limit the timing and regulate the dose of small molecules has allowed for unique insight into the tissue-specific requirements for copper in the developing embryo.
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Chemical modification and physical properties of lipid molecules have allowed lipid bilayers to be used in surface sensitive biosensing approaches, including the detection of biomolecules, proteins, and nucleic acids.
Optimization of a real-time quantitative PCR procedure exploiting the fluorescent DNA-binding molecule, Sybr Green, has allowed the measurement of annetocin transcript levels over a range covering six orders of magnitude.
Further, the use of these molecules in vivo has allowed us to reveal relatively inaccessible features of polyketide assembly, such as the timing of ring formation in the biosynthesis of the polyether antibiotic lasalocid A.
In addition, the topological analysis of the electron density provided by the Atom-in-Molecules, AIM, theory has allowed us to rationalize the stable conformers on the basis of bond critical points and ring critical points featuring intramolecular contacts.
The advent of single molecule fluorescence microscopy has allowed experimental molecular biophysics and biochemistry to transcend traditional ensemble measurements, where the behavior of individual proteins could not be precisely sampled.
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