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The effects of hydrophobic solutes on the structure of the surrounding water have been a topic of debate for almost 70 years. However, a consistent description of the physical insight into the causes of the anomalous thermodynamic properties of alcohol-water mixtures is lacking. Here we report experimental results that combined temperature-dependent linear and femtosecond infrared spectroscopy measurements to explore the water structural transformation in concentrated alcohol-water solutions. Experiments show that the enhancement of water structure arises around micro-hydrophobic interfaces at room temperature in the solutions. As temperature increases, this ordered water structure disappears and a surface topography dependent new disordered water structure arises at concentrated solutions of large alcohols. The water structural transformation is dependent on not only the length of the alkyl chain but also clustering of the alcohols. A more-ordered-than-water structure can transform into a less-ordered-than-water structure.
This article was published in the following journal.
Name: The journal of physical chemistry letters
Normally, a polymer network swells in a good solvent to form a gel but the gel shrinks in a poor solvent. Here, an abnormal phenomenon is reported: some hydrophobic gels significantly swell in water, ...
The air-water interface is an ideal platform to produce two-dimensional (2D) structures involving anything from simple organic molecules to supramolecular moieties by exploiting hydrophobic-hydrophili...
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Comparison of the capsular bag performance of the RayOne Hydrophobic Aspheric with the RayOne Aspheric
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Prospective, controlled, single-surgeon, single-center post-market clinical follow up study to investigate the clinical outcomes of a hydrophobic trifocal IOL (PhysIOL POD F GF)
A prospective randomized controlled clinical study to measure posterior capsular opacification, objective measurement of glistenings and intraocular lens tilt and decentration as well as v...
The purpose of this study is to evaluate whether hydrophobic intraocular lenses manufactured by aurolab are safe and effective in the surgical treatment of cataract.
Functional proteins that do not have unique, stable, folded, three-dimensional native structures or that possess non-ordered regions under physiological conditions. They are characterized by extraordinary structural flexibility and plasticity, which enable them to adopt different conformations in response to different stimuli or different interactions.
A replica technique in which cells are frozen to a very low temperature and cracked with a knife blade to expose the interior surfaces of the cells or cell membranes. The cracked cell surfaces are then freeze-dried to expose their constituents. The surfaces are now ready for shadowing to be viewed using an electron microscope. This method differs from freeze-fracturing in that no cryoprotectant is used and, thus, allows for the sublimation of water during the freeze-drying process to etch the surfaces.
The thermodynamic interaction between a substance and WATER.
Disruption of the secondary structure of nucleic acids by heat, extreme pH or chemical treatment. Double strand DNA is "melted" by dissociation of the non-covalent hydrogen bonds and hydrophobic interactions. Denatured DNA appears to be a single-stranded flexible structure. The effects of denaturation on RNA are similar though less pronounced and largely reversible.
A malignancy arising in uterine cervical epithelium and confined thereto, representing a continuum of histological changes ranging from well-differentiated CIN 1 (formerly, mild dysplasia) to severe dysplasia/carcinoma in situ, CIN 3. The lesion arises at the squamocolumnar cell junction at the transformation zone of the endocervical canal, with a variable tendency to develop invasive epidermoid carcinoma, a tendency that is enhanced by concomitant human papillomaviral infection. (Segen, Dictionary of Modern Medicine, 1992)