FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1989515624> ?p ?o ?g. }

• W1989515624 endingPage "223" @default.
• W1989515624 startingPage "212" @default.
• W1989515624 abstract "We have studied the adsorption of lysozyme layers at a hydrophobic silicon water interface using specular neutron reflection. The hydrophobic surface was obtained by self-assembly of a densely packed monolayer of octadecyltrichlorosilane (OTS) onto the natural silica layer on the smooth surface of a (111) silicon block. The effect of pH on the adsorbed lysozyme layer was examined at a constant lysozyme concentration of 0.03 g dm−3and at a constant ionic strength of 0.02 M. Reflectivity profiles at different pH show that adsorption is irreversible with respect to pH, the composition and structure of the final layer being dependent on the route by which the pH was achieved. The adsorbed protein layer was found to divide into approximately two regions, a densely packed thin layer next to the OTS surface and a diffuse thicker layer extending into the bulk solution. None of the dimensions of this structure corresponds to those of the globular protein in solution, suggesting that, unlike its adsorption at the hydrophilic silica/water interface, lysozyme is denatured at the OTS/water surface. The irreversible adsorption is explained by the combined interaction of the hydrophobic attraction of the hydrophobic fragments in lysozyme to the OTS surface and electrostatic repulsion within the adsorbed layer. The hydrophobic surface induces the exposure of hydrophobic fragments from the lysozyme assembly. The thickness of the dense layer suggests that the denatured protein adsorbs in the form of peptide chains with the hydrophobic amino acid side chains attached to the OTS surface with the hydrophilic side chains extending into the bulk solution. Since lysozyme is more stable at pH 7 than at pH 4, the difference in initial adsorption is dominated by the greater relative stability of lysozyme to denaturation at the higher pH. A change of pH from 7 to 4 reduces the stability of the protein to unfolding and results in more adsorption than when the pH is changed in the opposite direction. Solution pH also affects the net charges within the hydrophilic tail region and the structural distribution of the tail region was found to vary with pH." @default.
• W1989515624 created "2016-06-24" @default.
• W1989515624 creator A5018848206 @default.
• W1989515624 creator A5030131037 @default.
• W1989515624 creator A5070347237 @default.
• W1989515624 creator A5076516919 @default.
• W1989515624 creator A5080637942 @default.
• W1989515624 creator A5083921108 @default.
• W1989515624 date "1998-10-01" @default.
• W1989515624 modified "2023-09-29" @default.
• W1989515624 title "The Denaturation of Lysozyme Layers Adsorbed at the Hydrophobic Solid/Liquid Surface Studied by Neutron Reflection" @default.
• W1989515624 cites W1222485500 @default.
• W1989515624 cites W1973078822 @default.
• W1989515624 cites W1977065684 @default.
• W1989515624 cites W1981831765 @default.
• W1989515624 cites W1982229543 @default.
• W1989515624 cites W1984082275 @default.
• W1989515624 cites W1985011835 @default.
• W1989515624 cites W1987881455 @default.
• W1989515624 cites W1994342473 @default.
• W1989515624 cites W1996396673 @default.
• W1989515624 cites W1999035446 @default.
• W1989515624 cites W2011407545 @default.
• W1989515624 cites W2012866687 @default.
• W1989515624 cites W2013746255 @default.
• W1989515624 cites W2022379816 @default.
• W1989515624 cites W2022699083 @default.
• W1989515624 cites W2024004515 @default.
• W1989515624 cites W2044110936 @default.
• W1989515624 cites W2046441780 @default.
• W1989515624 cites W2054901765 @default.
• W1989515624 cites W2056911826 @default.
• W1989515624 cites W2065646045 @default.
• W1989515624 cites W2067918294 @default.
• W1989515624 cites W2068122641 @default.
• W1989515624 cites W2069690875 @default.
• W1989515624 cites W2073853284 @default.
• W1989515624 cites W2076773657 @default.
• W1989515624 cites W2080967072 @default.
• W1989515624 cites W2085561902 @default.
• W1989515624 cites W2091836140 @default.
• W1989515624 cites W2092405423 @default.
• W1989515624 cites W2144798802 @default.
• W1989515624 cites W2165566321 @default.
• W1989515624 cites W2169586329 @default.
• W1989515624 cites W2171095799 @default.
• W1989515624 doi "https://doi.org/10.1006/jcis.1998.5680" @default.
• W1989515624 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9761646" @default.
• W1989515624 hasPublicationYear "1998" @default.
• W1989515624 type Work @default.
• W1989515624 sameAs 1989515624 @default.
• W1989515624 citedByCount "137" @default.
• W1989515624 countsByYear W19895156242012 @default.
• W1989515624 countsByYear W19895156242013 @default.
• W1989515624 countsByYear W19895156242014 @default.
• W1989515624 countsByYear W19895156242015 @default.
• W1989515624 countsByYear W19895156242016 @default.
• W1989515624 countsByYear W19895156242017 @default.
• W1989515624 countsByYear W19895156242018 @default.
• W1989515624 countsByYear W19895156242019 @default.
• W1989515624 countsByYear W19895156242020 @default.
• W1989515624 countsByYear W19895156242021 @default.
• W1989515624 countsByYear W19895156242022 @default.
• W1989515624 countsByYear W19895156242023 @default.
• W1989515624 crossrefType "journal-article" @default.
• W1989515624 hasAuthorship W1989515624A5018848206 @default.
• W1989515624 hasAuthorship W1989515624A5030131037 @default.
• W1989515624 hasAuthorship W1989515624A5070347237 @default.
• W1989515624 hasAuthorship W1989515624A5076516919 @default.
• W1989515624 hasAuthorship W1989515624A5080637942 @default.
• W1989515624 hasAuthorship W1989515624A5083921108 @default.
• W1989515624 hasConcept C104015590 @default.
• W1989515624 hasConcept C121332964 @default.
• W1989515624 hasConcept C127413603 @default.
• W1989515624 hasConcept C132841051 @default.
• W1989515624 hasConcept C150394285 @default.
• W1989515624 hasConcept C152568617 @default.
• W1989515624 hasConcept C178790620 @default.
• W1989515624 hasConcept C1816345 @default.
• W1989515624 hasConcept C185592680 @default.
• W1989515624 hasConcept C2776966407 @default.
• W1989515624 hasConcept C2778645564 @default.
• W1989515624 hasConcept C2779227376 @default.
• W1989515624 hasConcept C42360764 @default.
• W1989515624 hasConcept C55493867 @default.
• W1989515624 hasConcept C62520636 @default.
• W1989515624 hasConcept C7070889 @default.
• W1989515624 hasConcept C8010536 @default.
• W1989515624 hasConcept C88001094 @default.
• W1989515624 hasConcept C90260826 @default.
• W1989515624 hasConceptScore W1989515624C104015590 @default.
• W1989515624 hasConceptScore W1989515624C121332964 @default.
• W1989515624 hasConceptScore W1989515624C127413603 @default.
• W1989515624 hasConceptScore W1989515624C132841051 @default.
• W1989515624 hasConceptScore W1989515624C150394285 @default.
• W1989515624 hasConceptScore W1989515624C152568617 @default.
• W1989515624 hasConceptScore W1989515624C178790620 @default.
• W1989515624 hasConceptScore W1989515624C1816345 @default.

• next