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Keratin was extracted from different segments of disposable waste chicken feathers (CF) including the whole feathers, calamus/rachis (β-sheet) and barbs/barbules (α-helix), using sodium sulfide and l -cysteine. The yield of extracted keratin from sodium sulfide and l -cysteine was ˜88% and ˜66% respectively. The mass ratio of feathers to reducing agent was 1:20 and the reaction temperature was 40 °C for 6 h. Concentration of keratin extracted by each method was measured using the Bradford assay. The protein extracted from each feather section was characterised using sodium dodecyl sulfate-polyacrylamide gel electrophoresis, vibrational spectroscopy including FTIR and Raman, nuclear magnetic resonance, and thermogravimetry. These results confirmed the keratin structures after each extraction methods. The study showed that α-helix and s-sheet based keratin could be extracted from CF using sodium sulfide and l -cysteine with high yields. This is the first report of CF keratin extraction using l -cysteine.

Here we reveal details of the interaction between human lysozyme proteins, both native and fibrils, and their water environment by intense terahertz time domain spectroscopy. With the aid of a rigorous dielectric model, we determine the amplitude and phase of the oscillating dipole induced by the THz field in the volume containing the protein and its hydration water. At low concentrations, the amplitude of this induced dipolar response decreases with increasing concentration. Beyond a certain threshold, marking the onset of the interactions between the extended hydration shells, the amplitude remains fixed but the phase of the induced dipolar response, which is initially in phase with the applied THz field, begins to change. The changes observed in the THz response reveal protein-protein interactions me-diated by extended hydration layers, which may control fibril formation and may have an important role in chemical recognition phenomena.

Spatially off-set Raman spectroscopy (SORS) offers non-invasive chemical characterisation of the sub-surface of various biological tissues as it permits the assessment of diffusely scattering samples at depths of several orders of magnitude deeper than conventional Raman spectroscopy. Chemicals such as glycogen, glucose, lactate and cortisol are predictors of meat quality, however detection of these chemicals is limited to the surface of meat using conventional Raman spectroscopy as their concentration is higher within the tissue. Here, we have used SORS to detect spectral bands for glycogen, lactate, glucose and cortisol beneath the surface of meat tissue by spiking. To our knowledge, this is the first report on this method for potential application in meat quality analysis. We further validate our SORS spectral results using chemometric analysis to determine chemical-specific spectral characteristics suitable for chemical identification. The chemometric analysis clearly shows distinction of spiked metabolites into four distinct groups, even for such chemically similar compounds as glucose, glycogen and lactate.

Monellin is a highly potent sweet-tasting protein but relatively little is known about how it interacts with the sweet taste receptor. We determined X-ray crystal structures of 3 single-chain monellin (MNEI) proteins with alterations at 2 core residues (G16A, V37A, and G16A/V37A) that induce 2- to 10-fold reductions in sweetness relative to the wild-type protein. Surprisingly, no changes were observed in the global protein fold or the positions of surface amino acids important for MNEI sweetness that could explain these differences in protein activity. Differential scanning calorimetry showed that while the thermal stability of each mutant MNEI was reduced, the least sweet mutant, G16A-MNEI, was not the least stable protein. In contrast, solution spectroscopic measurements revealed that changes in protein flexibility and the C-terminal structure correlate directly with protein activity. G16A mutation-induced disorder in the protein core is propagated via changes to hydrophobic interactions that disrupt the formation and/or position of a critical C-terminal poly-(L-proline) II helix. These findings suggest that MNEI interaction with the sweet taste receptor is highly sensitive to the relative positions of key residues across its protein surface and that loss of sweetness in G16A-MNEI may result from an increased entropic cost of binding.

The ability to detect chirality gives stereochemically attuned nanosensors the potential to revolutionise the study of biomolecular processes. Such devices may structurally characterise the mechanisms of protein-ligand binding, the intermediates of amyloidogenic diseases and the effects of phosphorylation and glycosylation. We demonstrate that single nanoparticle plasmonic reporters, or nanotags, can enable a stereochemical response to be transmitted from a chiral analyte to an achiral benzotriazole dye molecule in the vicinity of a plasmon resonance from an achiral metallic nanostructure. The transfer of chirality was verified by the measurement of mirror image surface enhanced resonance Raman optical activity spectra for the two enantiomers of each of ribose and tryptophan. Computational modelling confirms these observations and reveals the novel chirality transfer mechanism responsible. This is the first report of colloidal metal nanoparticles in the form of single plasmonic substrates displaying an intrinsic chiral sensitivity once attached to a chiral molecule.

We present surface enhanced Raman optical activity (SEROA), as well as Raman, SERS and ROA, spectra of D- and L-ribose. By employing a gel forming polyacrylic acid to control colloid aggregation and associated birefringent artefacts we observe the first definitive proof of SEROA through measurement of mirror image bands for the two enantiomers.