FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1567458024> ?p ?o ?g. }

• W1567458024 abstract "This thesis aimed at revealing the substrate specificity of the bacterial ABC-transporter, Sav1866. For this purpose the ABC-transporter was reconstituted into model membranes and characterized in terms of basal and drug induced ATPase activity, respectively. The results were compared with analogous data from the well characterized human ABC-transporter P-glycoprotein which is a close structural homologue of Sav1866. Sav1866 is able to transport structurally very diverse substrates as P-gp, binds them however with a different affinity.Moreover we found that the ATPase activity of Sav1866 was not only stimulated by drugs, but also by an intrinsic cationic lipid, lysyl-DPPG. Our results indicated that Sav1866 may be involved in the transport of the cationic lipid to the outer leaflet of the membrane.Beside the characterization of the ATPase activity of Sav1866 the reconstitution process was investigated. Reconstitution of membrane proteins is a semi-empirical task due to the lack of quantitative analysis of the process. Model membrane vesicles were therefore solubilized with a non-ionic detergent (C12E8). The detergent was removed with the help of Bio-Beads SM2 from Biorad. The vesicle size during the reconstitution process was directly measured by means of dynamic light scattering. Isothermal titrations calorimetry was used to quantify the degree of detergents removal. We found that still 9 mol% detergents per lipid were left after treatment. Moreover the effect of a positively charged compound, dodecyltrimethylammonium chloride (DTAC), on neutral and negatively charged membranes was investigated in detail. The thermodynamic properties of DTAC were compared with the negatively charged counterpart sodium dodecyl sulphate (SDS). After correction for electrostatic contribution we found that SDS incorporates 10-15 times better into a membrane than DTAC, what is explained by the smaller headgroup of SDS. However SDS solubilizes the membrane at much lower critical ratios than DTAC. We revealed the movement of the POPC headgroup upon incorporation of the positively or the negatively charged detergent molecule by means of 2H-NMR. We found that upon incorproration of the cationic detergent the choline moiety of the lipid moves toward the plane of the bilayer, and vice versa for the anionic molecule. We conclude that the solubilization behaviour of the lipid membranes by charged detergnets is not only dependent on the structural properties of the detergents but also on the effective charge of the detergent molecule.As a last point we investigated the critical role of TipF in assembly of the flagellum in Caulobacter crescentus. ITC experiemnts were performed to give insight into the binding properties of c-di-GMP with TipF. C-di-GMP is a second messenger involved in controlling growth and developpement in bacteriae. In vivo studies showed that TipF binds c-di-GMP, the binding constant was however unknown. We showed that c-di-GMP binds TipF with high affinity (Kd = 0.4 µM)." @default.
• W1567458024 created "2016-06-24" @default.
• W1567458024 creator A5081265038 @default.
• W1567458024 date "2012-01-01" @default.
• W1567458024 modified "2023-09-27" @default.
• W1567458024 title "On the interaction of cationic compounds with ABC-transporters and lipid membranes" @default.
• W1567458024 cites W1532738042 @default.
• W1567458024 cites W1608154971 @default.
• W1567458024 cites W1965724769 @default.
• W1567458024 cites W1969999093 @default.
• W1567458024 cites W1971383947 @default.
• W1567458024 cites W1971758614 @default.
• W1567458024 cites W1972995661 @default.
• W1567458024 cites W1975328921 @default.
• W1567458024 cites W1981151214 @default.
• W1567458024 cites W1981177273 @default.
• W1567458024 cites W1981388811 @default.
• W1567458024 cites W1983739049 @default.
• W1567458024 cites W1986516374 @default.
• W1567458024 cites W1987503756 @default.
• W1567458024 cites W1987759704 @default.
• W1567458024 cites W1988691170 @default.
• W1567458024 cites W1989178650 @default.
• W1567458024 cites W1995861782 @default.
• W1567458024 cites W1998428612 @default.
• W1567458024 cites W1999085787 @default.
• W1567458024 cites W2000764014 @default.
• W1567458024 cites W2005046011 @default.
• W1567458024 cites W2007651537 @default.
• W1567458024 cites W2010367291 @default.
• W1567458024 cites W2010508088 @default.
• W1567458024 cites W2012334764 @default.
• W1567458024 cites W2012957144 @default.
• W1567458024 cites W2016329805 @default.
• W1567458024 cites W2016528090 @default.
• W1567458024 cites W2017722783 @default.
• W1567458024 cites W2019063268 @default.
• W1567458024 cites W2019356890 @default.
• W1567458024 cites W2025561938 @default.
• W1567458024 cites W2027568599 @default.
• W1567458024 cites W2036194106 @default.
• W1567458024 cites W2036195365 @default.
• W1567458024 cites W2038250741 @default.
• W1567458024 cites W2041139207 @default.
• W1567458024 cites W2042885165 @default.
• W1567458024 cites W2048375366 @default.
• W1567458024 cites W2049645834 @default.
• W1567458024 cites W2053726952 @default.
• W1567458024 cites W2053843567 @default.
• W1567458024 cites W2055264458 @default.
• W1567458024 cites W2057168584 @default.
• W1567458024 cites W2070154306 @default.
• W1567458024 cites W2074559590 @default.
• W1567458024 cites W2075305909 @default.
• W1567458024 cites W2077231484 @default.
• W1567458024 cites W2082047232 @default.
• W1567458024 cites W2082111171 @default.
• W1567458024 cites W2088051616 @default.
• W1567458024 cites W2088156634 @default.
• W1567458024 cites W2090841445 @default.
• W1567458024 cites W2101223910 @default.
• W1567458024 cites W2102762507 @default.
• W1567458024 cites W2106064685 @default.
• W1567458024 cites W2119586900 @default.
• W1567458024 cites W2119892971 @default.
• W1567458024 cites W2126102313 @default.
• W1567458024 cites W2128294490 @default.
• W1567458024 cites W2142703076 @default.
• W1567458024 cites W2157393167 @default.
• W1567458024 cites W2161983628 @default.
• W1567458024 cites W2162272877 @default.
• W1567458024 cites W2214845106 @default.
• W1567458024 cites W2337332525 @default.
• W1567458024 cites W2494402508 @default.
• W1567458024 cites W2494702712 @default.
• W1567458024 cites W2570342360 @default.
• W1567458024 cites W2799189166 @default.
• W1567458024 cites W574061524 @default.
• W1567458024 cites W80727568 @default.
• W1567458024 cites W1985207145 @default.
• W1567458024 cites W2299103077 @default.
• W1567458024 doi "https://doi.org/10.5451/unibas-005941811" @default.
• W1567458024 hasPublicationYear "2012" @default.
• W1567458024 type Work @default.
• W1567458024 sameAs 1567458024 @default.
• W1567458024 citedByCount "0" @default.
• W1567458024 crossrefType "dissertation" @default.
• W1567458024 hasAuthorship W1567458024A5081265038 @default.
• W1567458024 hasConcept C104317684 @default.
• W1567458024 hasConcept C125501631 @default.
• W1567458024 hasConcept C12554922 @default.
• W1567458024 hasConcept C130316041 @default.
• W1567458024 hasConcept C149011108 @default.
• W1567458024 hasConcept C156911925 @default.
• W1567458024 hasConcept C178790620 @default.
• W1567458024 hasConcept C181199279 @default.
• W1567458024 hasConcept C183882617 @default.
• W1567458024 hasConcept C184866935 @default.
• W1567458024 hasConcept C185592680 @default.
• W1567458024 hasConcept C23265538 @default.

• next