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• W2086365152 abstract "This study reports on the influence of nonionic cosolvents on the interfacial structure of ribonuclease A (RNase) adsorbed at the air-water interface. We applied X-ray reflectometry to obtain detailed volume fraction profiles of the adsorbed layers and to follow the effect of glycerol and urea on the adsorbate structure as a function of cosolvent concentration. Under all conditions studied, the adsorbed RNase layer maintains its compact shape, and the adsorbed RNase molecules adopt a flat-on orientation at the interface. Both kosmotropic glycerol and chaotropic urea exert profound effects on the adsorbate: The surface excess decreases linearly with glycerol content and is also reduced at low urea concentration. However, at high urea concentration, parts of the adsorbed layer are dehydrated and become exposed to air. The electron density and volume fraction profiles of the adsorbed protein provide clear evidence that these effects are ruled by different mechanisms." @default.
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• W2086365152 date "2010-08-17" @default.
• W2086365152 modified "2023-10-18" @default.
• W2086365152 title "Effect of Urea and Glycerol on the Adsorption of Ribonuclease A at the Air−Water Interface" @default.
• W2086365152 doi "https://doi.org/10.1021/la102222z" @default.
• W2086365152 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20695588" @default.
• W2086365152 hasPublicationYear "2010" @default.
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