FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2143621044> ?p ?o ?g. }

• W2143621044 endingPage "46" @default.
• W2143621044 startingPage "38" @default.
• W2143621044 abstract "Thermal unfolding experiments on bacteriorhodopsin in mixed Phospholipid/detergent micelles were performed. Bacteriorhodopsin was extracted from the purple membrane in a denatured state and then renatured in the micellar system. The purpose of this study was to compare the changes, if any, in the structure and stability of a membrane protein that has folded in a nonnative environment with results obtained on the native system, i.e., the purple membrane. The purple membrane crystalline lattice is an added factor that may influence the structural stability of bacteriorhodopsin. Micelles containing bacteriorhodopsin are uniformly sized disks 105 ± 13 Å in diameter (by electron microscopy) and have an estimated molecular mass of 210 kDa (by gel filtration HPLC). The near-UV CD spectra (which is indicative of tertiary structure) for micellar bacteriorhodopsin and the purple membrane are very similar. In the visible CD region of retinal absorption, the double band seen in the spectrum of the purple membrane is replaced with a broad positive band for micellar bacteriorhodopsin, indicating that in micelles, bacteriorhodopsin is monomeric. The plot of denaturational temperature vs. pH for micellar bacteriorhodopsin is displaced downward on the temperature axis, illustrating the lower thermal stability of micellar bacteriorhodopsin when compared to the purple membrane at the same pH. Even though micellar bacteriorhodopsin is less stable, similar changes in response to pH and temperature are seen in the visible absorption spectra of micellar bacteriorhodopsin and the purple membrane. This demonstrates that changes in the protonation state or temperature have a similar affect on the local environment of the chromophore and the protein conformation. We conclude that the tertiary structure of the bacteriorhodopsin monomer is essentially the same in micelles and the purple membrane. On the other hand, in the synthetic mixed micelle system, the packing between the nonnative amphiphiles and bacteriorhodopsin is probably not optimal, protein-protein interactions have been lost, and thehelical packing may be looser because the crystalline lattice is absent. Itis likely that a combination of these effects leads to the decreased stability of micellar bacteriorhodopsin." @default.
• W2143621044 created "2016-06-24" @default.
• W2143621044 creator A5018347128 @default.
• W2143621044 creator A5043926357 @default.
• W2143621044 creator A5058574401 @default.
• W2143621044 creator A5064031709 @default.
• W2143621044 date "1989-01-01" @default.
• W2143621044 modified "2023-09-23" @default.
• W2143621044 title "Structure and thermal stability of monomeric bacteriorhodopsin in mixed pospholipid/detergent micelles" @default.
• W2143621044 cites W105717962 @default.
• W2143621044 cites W12268373 @default.
• W2143621044 cites W1496368635 @default.
• W2143621044 cites W1499122356 @default.
• W2143621044 cites W1502816207 @default.
• W2143621044 cites W1537290919 @default.
• W2143621044 cites W1540419168 @default.
• W2143621044 cites W1548179807 @default.
• W2143621044 cites W1579264578 @default.
• W2143621044 cites W1582740601 @default.
• W2143621044 cites W1719405009 @default.
• W2143621044 cites W1858234177 @default.
• W2143621044 cites W1968543928 @default.
• W2143621044 cites W1969240712 @default.
• W2143621044 cites W1983638771 @default.
• W2143621044 cites W1985433277 @default.
• W2143621044 cites W1988311363 @default.
• W2143621044 cites W1991086115 @default.
• W2143621044 cites W1994784785 @default.
• W2143621044 cites W2000668868 @default.
• W2143621044 cites W2008754347 @default.
• W2143621044 cites W2016209691 @default.
• W2143621044 cites W2021549396 @default.
• W2143621044 cites W2023100979 @default.
• W2143621044 cites W2030052070 @default.
• W2143621044 cites W2050292589 @default.
• W2143621044 cites W2079210381 @default.
• W2143621044 cites W2079436664 @default.
• W2143621044 cites W2089466608 @default.
• W2143621044 cites W2094331619 @default.
• W2143621044 cites W2111843801 @default.
• W2143621044 cites W2122245702 @default.
• W2143621044 cites W2177743694 @default.
• W2143621044 cites W2415401766 @default.
• W2143621044 doi "https://doi.org/10.1002/prot.340050106" @default.
• W2143621044 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2748571" @default.
• W2143621044 hasPublicationYear "1989" @default.
• W2143621044 type Work @default.
• W2143621044 sameAs 2143621044 @default.
• W2143621044 citedByCount "81" @default.
• W2143621044 countsByYear W21436210442012 @default.
• W2143621044 countsByYear W21436210442013 @default.
• W2143621044 countsByYear W21436210442014 @default.
• W2143621044 countsByYear W21436210442015 @default.
• W2143621044 countsByYear W21436210442016 @default.
• W2143621044 countsByYear W21436210442017 @default.
• W2143621044 countsByYear W21436210442018 @default.
• W2143621044 countsByYear W21436210442019 @default.
• W2143621044 countsByYear W21436210442020 @default.
• W2143621044 countsByYear W21436210442021 @default.
• W2143621044 countsByYear W21436210442022 @default.
• W2143621044 countsByYear W21436210442023 @default.
• W2143621044 crossrefType "journal-article" @default.
• W2143621044 hasAuthorship W2143621044A5018347128 @default.
• W2143621044 hasAuthorship W2143621044A5043926357 @default.
• W2143621044 hasAuthorship W2143621044A5058574401 @default.
• W2143621044 hasAuthorship W2143621044A5064031709 @default.
• W2143621044 hasConcept C11268172 @default.
• W2143621044 hasConcept C113196181 @default.
• W2143621044 hasConcept C166940927 @default.
• W2143621044 hasConcept C178790620 @default.
• W2143621044 hasConcept C184651966 @default.
• W2143621044 hasConcept C185592680 @default.
• W2143621044 hasConcept C189542057 @default.
• W2143621044 hasConcept C41625074 @default.
• W2143621044 hasConcept C43617362 @default.
• W2143621044 hasConcept C521977710 @default.
• W2143621044 hasConcept C55493867 @default.
• W2143621044 hasConcept C59061564 @default.
• W2143621044 hasConcept C75473681 @default.
• W2143621044 hasConcept C8010536 @default.
• W2143621044 hasConceptScore W2143621044C11268172 @default.
• W2143621044 hasConceptScore W2143621044C113196181 @default.
• W2143621044 hasConceptScore W2143621044C166940927 @default.
• W2143621044 hasConceptScore W2143621044C178790620 @default.
• W2143621044 hasConceptScore W2143621044C184651966 @default.
• W2143621044 hasConceptScore W2143621044C185592680 @default.
• W2143621044 hasConceptScore W2143621044C189542057 @default.
• W2143621044 hasConceptScore W2143621044C41625074 @default.
• W2143621044 hasConceptScore W2143621044C43617362 @default.
• W2143621044 hasConceptScore W2143621044C521977710 @default.
• W2143621044 hasConceptScore W2143621044C55493867 @default.
• W2143621044 hasConceptScore W2143621044C59061564 @default.
• W2143621044 hasConceptScore W2143621044C75473681 @default.
• W2143621044 hasConceptScore W2143621044C8010536 @default.
• W2143621044 hasIssue "1" @default.
• W2143621044 hasLocation W21436210441 @default.
• W2143621044 hasLocation W21436210442 @default.
• W2143621044 hasOpenAccess W2143621044 @default.

• next