FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2028162334> ?p ?o ?g. }

• W2028162334 endingPage "13132" @default.
• W2028162334 startingPage "13122" @default.
• W2028162334 abstract "The interaction of cytochrome c with anionic lipid vesicles of DOPS induces an extensive disruption of the native structure of the protein. The kinetics of this lipid-induced unfolding process were investigated in a series of fluorescence- and absorbance-detected stopped-flow measurements. The results show that the tightly packed native structure of cytochrome c is disrupted at a rate of ∼1.5 s-1 (independent of protein and lipid concentration), leading to the formation of a lipid-inserted denatured state (DL). Comparison with the expected rate of unfolding in solution (∼2 × 10-3 s-1 at pH 5.0 in the absence of denaturant) suggests that the lipid environment dramatically accelerates the structural unfolding process of cytochrome c. We propose that this acceleration is in part due to the low effective pH in the vicinity of the lipid headgroups. This hypothesis was tested by comparative kinetic measurements of acid unfolding of cytochrome c in solution. Our absorbance and fluorescence kinetic data, combined with a well-characterized mechanism for folding/unfolding of cytochrome c in solution, allow us to propose a kinetic mechanism for cytochrome c unfolding at the membrane surface. Binding of native cytochrome c in water (NW) to DOPS vesicles is driven by the electrostatic interaction between positively charged residues in the protein and the negatively charged lipid headgroups on the membrane surface. This binding step occurs within the dead time of the stopped-flow experiments (<2 ms), where a membrane-associated native state (NS) is formed. Unfolding of NS driven by the acidic environment at the membrane surface is proposed to occur via a native-like intermediate lacking Met 80 ligation (MS), as previously observed during unfolding in solution. The overall unfolding process (NS → DL) is limited by the rate of disruption of the hydrophobic core in MS. Equilibrium spectroscopic measurements by near-IR and Soret absorbance, fluorescence, and circular dichroism showed that DL has native-like helical secondary structure, but shows no evidence for specific tertiary interactions. This lipid-denatured equilibrium state (DL) is clearly more extensively unfolded than the A-state in solution, but is distinct from the unfolded protein in water (UW), which has no stable secondary structure." @default.
• W2028162334 created "2016-06-24" @default.
• W2028162334 creator A5006585307 @default.
• W2028162334 creator A5035080483 @default.
• W2028162334 creator A5065585246 @default.
• W2028162334 creator A5073916482 @default.
• W2028162334 date "1997-10-01" @default.
• W2028162334 modified "2023-10-17" @default.
• W2028162334 title "Structural and Kinetic Description of Cytochrome <i>c</i> Unfolding Induced by the Interaction with Lipid Vesicles" @default.
• W2028162334 cites W1499452131 @default.
• W2028162334 cites W1508039024 @default.
• W2028162334 cites W1531038433 @default.
• W2028162334 cites W1980400933 @default.
• W2028162334 cites W1981063713 @default.
• W2028162334 cites W1983015842 @default.
• W2028162334 cites W2047039535 @default.
• W2028162334 cites W2050896032 @default.
• W2028162334 cites W2079564988 @default.
• W2028162334 cites W2093545639 @default.
• W2028162334 cites W2154926071 @default.
• W2028162334 cites W2209250776 @default.
• W2028162334 doi "https://doi.org/10.1021/bi971235z" @default.
• W2028162334 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9335575" @default.
• W2028162334 hasPublicationYear "1997" @default.
• W2028162334 type Work @default.
• W2028162334 sameAs 2028162334 @default.
• W2028162334 citedByCount "136" @default.
• W2028162334 countsByYear W20281623342012 @default.
• W2028162334 countsByYear W20281623342013 @default.
• W2028162334 countsByYear W20281623342014 @default.
• W2028162334 countsByYear W20281623342015 @default.
• W2028162334 countsByYear W20281623342016 @default.
• W2028162334 countsByYear W20281623342017 @default.
• W2028162334 countsByYear W20281623342018 @default.
• W2028162334 countsByYear W20281623342019 @default.
• W2028162334 countsByYear W20281623342020 @default.
• W2028162334 countsByYear W20281623342021 @default.
• W2028162334 countsByYear W20281623342022 @default.
• W2028162334 crossrefType "journal-article" @default.
• W2028162334 hasAuthorship W2028162334A5006585307 @default.
• W2028162334 hasAuthorship W2028162334A5035080483 @default.
• W2028162334 hasAuthorship W2028162334A5065585246 @default.
• W2028162334 hasAuthorship W2028162334A5073916482 @default.
• W2028162334 hasConcept C121332964 @default.
• W2028162334 hasConcept C12554922 @default.
• W2028162334 hasConcept C130316041 @default.
• W2028162334 hasConcept C148898269 @default.
• W2028162334 hasConcept C181199279 @default.
• W2028162334 hasConcept C185592680 @default.
• W2028162334 hasConcept C2780768313 @default.
• W2028162334 hasConcept C28859421 @default.
• W2028162334 hasConcept C29311851 @default.
• W2028162334 hasConcept C41625074 @default.
• W2028162334 hasConcept C43617362 @default.
• W2028162334 hasConcept C55493867 @default.
• W2028162334 hasConcept C62520636 @default.
• W2028162334 hasConcept C8010536 @default.
• W2028162334 hasConcept C86803240 @default.
• W2028162334 hasConcept C91881484 @default.
• W2028162334 hasConcept C98015330 @default.
• W2028162334 hasConceptScore W2028162334C121332964 @default.
• W2028162334 hasConceptScore W2028162334C12554922 @default.
• W2028162334 hasConceptScore W2028162334C130316041 @default.
• W2028162334 hasConceptScore W2028162334C148898269 @default.
• W2028162334 hasConceptScore W2028162334C181199279 @default.
• W2028162334 hasConceptScore W2028162334C185592680 @default.
• W2028162334 hasConceptScore W2028162334C2780768313 @default.
• W2028162334 hasConceptScore W2028162334C28859421 @default.
• W2028162334 hasConceptScore W2028162334C29311851 @default.
• W2028162334 hasConceptScore W2028162334C41625074 @default.
• W2028162334 hasConceptScore W2028162334C43617362 @default.
• W2028162334 hasConceptScore W2028162334C55493867 @default.
• W2028162334 hasConceptScore W2028162334C62520636 @default.
• W2028162334 hasConceptScore W2028162334C8010536 @default.
• W2028162334 hasConceptScore W2028162334C86803240 @default.
• W2028162334 hasConceptScore W2028162334C91881484 @default.
• W2028162334 hasConceptScore W2028162334C98015330 @default.
• W2028162334 hasIssue "42" @default.
• W2028162334 hasLocation W20281623341 @default.
• W2028162334 hasLocation W20281623342 @default.
• W2028162334 hasOpenAccess W2028162334 @default.
• W2028162334 hasPrimaryLocation W20281623341 @default.
• W2028162334 hasRelatedWork W131467418 @default.
• W2028162334 hasRelatedWork W1967895359 @default.
• W2028162334 hasRelatedWork W1983928627 @default.
• W2028162334 hasRelatedWork W2053111326 @default.
• W2028162334 hasRelatedWork W2062101022 @default.
• W2028162334 hasRelatedWork W2087418933 @default.
• W2028162334 hasRelatedWork W2335596810 @default.
• W2028162334 hasRelatedWork W2363991044 @default.
• W2028162334 hasRelatedWork W285885149 @default.
• W2028162334 hasRelatedWork W2088718888 @default.
• W2028162334 hasVolume "36" @default.
• W2028162334 isParatext "false" @default.
• W2028162334 isRetracted "false" @default.
• W2028162334 magId "2028162334" @default.
• W2028162334 workType "article" @default.