Publications by authors named "Samantha L Miller"

Although all hexose sugars share the same chemical formula, CHO, subtle differences in their stereochemical structures lead to their various biological roles. Due to their prominent role in metabolism, hexose sugars are commonly found in nanoconfined environments. The complexity of authentic nanoconfined biological environments makes it challenging to study how confinement affects their behavior.

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The balance between ion solvation and ion pairing in aqueous solutions modulates chemical and physical processes from catalysis to protein folding. Yet, despite more than a century of investigation, experimental determination of the distribution of ion-solvation and ion-pairing states remains elusive, even for archetypal systems like aqueous alkali halides. Here, we combine nuclear magnetic resonance (NMR) spectroscopy and multiscale modeling to disentangle ion-solvent interactions from ion pairing in aqueous sodium fluoride solutions.

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Confining water to nanosized spaces creates a unique environment that can change water's structural and dynamic properties. When ions are present in these nanoscopic spaces, the limited number of water molecules and short screening length can dramatically affect how ions are distributed compared to the homogeneous distribution assumed in bulk aqueous solution. Here, we demonstrate that the chemical shift observed in F NMR spectroscopy of fluoride anion, F, probes the location of sodium ions, Na, confined in reverse micelles prepared from AOT (sodium dioctyl sulfosuccinate) surfactants.

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Neanderthals, our closest extinct relatives, lived in western Eurasia from 400,000 years ago until they went extinct around 40,000 years ago. DNA retrieved from ancient specimens revealed that Neanderthals mated with modern human contemporaries. As a consequence, introgressed Neanderthal DNA survives scattered across the human genome such that 1-4% of the genome of present-day people outside Africa are inherited from Neanderthal ancestors.

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Aside from its prominent role in the excretory system, urea is also a known protein denaturant. Here, we characterize urea as it behaves in confined spaces of AOT (sodium bis(2-ethylhexyl) sulfosuccinate) reverse micelles as a model of tight, confined spaces found at the subcellular level. Dynamic light scattering revealed that low temperatures (275 K) caused the smallest of the reverse micelle sizes, = 10, to destabilize and dramatically increase in apparent hydrodynamic diameter.

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In bulk aqueous environments, the exchange of protons between labile hydroxyl groups typically occurs easily and quickly. Nanoconfinement can dramatically change this normally facile process. Through exchange spectroscopy (EXSY) NMR measurements, we observe that nanoconfinement of glucose and water within AOT (sodium bis(2-ethylhexyl) sulfosuccinate) reverse micelles raises the energy barrier to labile hydrogen exchange, which suggests a disruption of the hydrogen bond network.

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Herpes simplex virus-1 (HSV-1) is a human pathogen that utilizes several strategies to circumvent the host immune response. An immune evasion mechanism employed by HSV-1 is retention of interleukin-1β (IL-1β) in the intracellular space, which blocks the pro-inflammatory activity of IL-1β. Here we report that HSV-1-infected keratinocytes actively release the also pro-inflammatory IL-1α, preserving the ability of infected cells to signal danger to the surrounding tissue.

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