FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2057262491> ?p ?o ?g. }

• W2057262491 endingPage "490" @default.
• W2057262491 startingPage "474" @default.
• W2057262491 abstract "The interaction between a positively charged peptide (poly-l-lysine) and model membranes containing charged lipids has been investigated. Conformational changes of the polypeptide as well as changes in the membrane lipid distribution were observed upon lipid-protein agglutination: 1. The strong binding of polylysine is shown directly by the use of spin-labelled polypeptide. Upon binding to phosphatidic acid a shift in the hyperfine coupling constant from 16.5 to 14.6 Oe is observed. The spectrum of the lipid-bound peptide is superimposed on the spectrum of polylysine in solution. Half of the lysine groups are bound to the charged membranes. A change in the conformation of polylysine from a random coil to a partially ordered configuration is suggested. 2. Spin labelling of the lipid component gives evidence concerning the molecular organization of a lipid mixture containing charged phosphatidic acid. Addition of polylysine induces the formation of crystalline patches of bound phosphatidic acid. 3. Excimer forming pyrene decanoic acid has been employed. Addition of positively charged polylysine (pH 9.0) to phosphatidic acid membranes increases the transition temperature of the lipid from Tt = 50 to Tt = 62°C. Thus, a lipid segregation of lipid into regions of phosphatidic acid bound to the peptide which differ in their microviscosity from the surrounding membrane is induced. One lysine group binds one phosphatidic acid molecule, but only half of the phosphatidic acid is bound. 4. Direct evidence for charge-induced domain formation in lipid mixtures containing phosphatidic acid is given by electron microscopy. Addition of polylysine leads to a change in the surface curvature of the bound charged lipid. The domain size is estimated from the electron micrographs. The number of domains present is dependent on both the ratio of charged to uncharged lipids as well as on the amount of polylysine added to the vesicles. The size of the domains is not dependent on membrane composition. However, the size seems to increase in a stepwise manner that is correlated with a multiple of the area covered by one polylysine molecule." @default.
• W2057262491 created "2016-06-24" @default.
• W2057262491 creator A5000919967 @default.
• W2057262491 creator A5006986555 @default.
• W2057262491 date "1978-06-01" @default.
• W2057262491 modified "2023-09-27" @default.
• W2057262491 title "Binding of polylysine to charged bilayer membranes. Molecular organization of a lipid · peptide complex" @default.
• W2057262491 cites W1966680835 @default.
• W2057262491 cites W1980297983 @default.
• W2057262491 cites W1980716566 @default.
• W2057262491 cites W1987639618 @default.
• W2057262491 cites W1991655565 @default.
• W2057262491 cites W1998167510 @default.
• W2057262491 cites W2001760316 @default.
• W2057262491 cites W2042026091 @default.
• W2057262491 cites W2042971347 @default.
• W2057262491 cites W2049281931 @default.
• W2057262491 cites W2050093743 @default.
• W2057262491 cites W2054959035 @default.
• W2057262491 cites W2064048353 @default.
• W2057262491 cites W2067909010 @default.
• W2057262491 cites W2070046433 @default.
• W2057262491 cites W2073597941 @default.
• W2057262491 cites W2084255385 @default.
• W2057262491 cites W2093397934 @default.
• W2057262491 cites W2120644189 @default.
• W2057262491 cites W2300647647 @default.
• W2057262491 doi "https://doi.org/10.1016/0005-2736(78)90241-9" @default.
• W2057262491 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/207323" @default.
• W2057262491 hasPublicationYear "1978" @default.
• W2057262491 type Work @default.
• W2057262491 sameAs 2057262491 @default.
• W2057262491 citedByCount "145" @default.
• W2057262491 countsByYear W20572624912012 @default.
• W2057262491 countsByYear W20572624912013 @default.
• W2057262491 countsByYear W20572624912014 @default.
• W2057262491 countsByYear W20572624912015 @default.
• W2057262491 countsByYear W20572624912016 @default.
• W2057262491 countsByYear W20572624912018 @default.
• W2057262491 countsByYear W20572624912019 @default.
• W2057262491 countsByYear W20572624912020 @default.
• W2057262491 countsByYear W20572624912021 @default.
• W2057262491 crossrefType "journal-article" @default.
• W2057262491 hasAuthorship W2057262491A5000919967 @default.
• W2057262491 hasAuthorship W2057262491A5006986555 @default.
• W2057262491 hasConcept C12554922 @default.
• W2057262491 hasConcept C185592680 @default.
• W2057262491 hasConcept C2776909261 @default.
• W2057262491 hasConcept C2778918659 @default.
• W2057262491 hasConcept C2779281246 @default.
• W2057262491 hasConcept C2780075363 @default.
• W2057262491 hasConcept C39944091 @default.
• W2057262491 hasConcept C41625074 @default.
• W2057262491 hasConcept C55493867 @default.
• W2057262491 hasConcept C8010536 @default.
• W2057262491 hasConcept C86803240 @default.
• W2057262491 hasConceptScore W2057262491C12554922 @default.
• W2057262491 hasConceptScore W2057262491C185592680 @default.
• W2057262491 hasConceptScore W2057262491C2776909261 @default.
• W2057262491 hasConceptScore W2057262491C2778918659 @default.
• W2057262491 hasConceptScore W2057262491C2779281246 @default.
• W2057262491 hasConceptScore W2057262491C2780075363 @default.
• W2057262491 hasConceptScore W2057262491C39944091 @default.
• W2057262491 hasConceptScore W2057262491C41625074 @default.
• W2057262491 hasConceptScore W2057262491C55493867 @default.
• W2057262491 hasConceptScore W2057262491C8010536 @default.
• W2057262491 hasConceptScore W2057262491C86803240 @default.
• W2057262491 hasIssue "3" @default.
• W2057262491 hasLocation W20572624911 @default.
• W2057262491 hasLocation W20572624912 @default.
• W2057262491 hasOpenAccess W2057262491 @default.
• W2057262491 hasPrimaryLocation W20572624911 @default.
• W2057262491 hasRelatedWork W1982949069 @default.
• W2057262491 hasRelatedWork W2027609635 @default.
• W2057262491 hasRelatedWork W2031704752 @default.
• W2057262491 hasRelatedWork W2093666789 @default.
• W2057262491 hasRelatedWork W2580174306 @default.
• W2057262491 hasRelatedWork W2751948777 @default.
• W2057262491 hasRelatedWork W3110055093 @default.
• W2057262491 hasRelatedWork W3171224921 @default.
• W2057262491 hasRelatedWork W4200312925 @default.
• W2057262491 hasRelatedWork W4307961400 @default.
• W2057262491 hasVolume "509" @default.
• W2057262491 isParatext "false" @default.
• W2057262491 isRetracted "false" @default.
• W2057262491 magId "2057262491" @default.
• W2057262491 workType "article" @default.