Matches in SemOpenAlex for { <https://semopenalex.org/work/W1973737539> ?p ?o ?g. }
Showing items 1 to 83 of
83
with 100 items per page.
- W1973737539 endingPage "569a" @default.
- W1973737539 startingPage "569a" @default.
- W1973737539 abstract "Protein folding occurs between a well-defined fully folded native state and a structurally much less studied fully unfolded state. We use denaturant m values and changes in heat capacity ΔCp to probe folding transitions in photoactive yellow protein (PYP). PYP is a bacterial photoreceptor that exhibits rhodopsin-like photochemistry based on the trans to cis photoisomeriation of its covalently attached p-coumaric acid (pCA) chromophore. We report strong effects of the isomerization state of the pCA on the residual structure of the “fully unfolded” state of PYP by comparing the unfolding of two partially unfolded states of PYP: the acid-denatured state pBdark, which contains trans-pCA, and the partially unfolded pB photocycle intermediate, which contains cis-pCA. Our characterization of pBdark by circular dichroism spectroscopy and quenching of aromatic fluorescence indicates a strong loss of tertiary structure in pBdark. Despite its low tertiary structure content, pBdark retains considerable cooperativity for unfolding. As expected, the unfolding of pBdark is associated with values for denaturant m value and ΔCp that are smaller than those for the native pG state of PYP. A range of published studies show that the pB state is partially unfolded. We characterize the pB state based on its specific cold denaturation. Despite its partially unfolded nature, we find that the denaturant m values and ΔCp values for unfolding of the pB state are essentially the same as those for the native pG state. These results provide experimental evidence that pCA trans to cis photoisomerization causes significant loss of residual structure in the “fully unfolded” state of PYP. Such large changes in the residual structure of the fully unfolded states have important implications for describing and understanding protein folding." @default.
- W1973737539 created "2016-06-24" @default.
- W1973737539 creator A5008471776 @default.
- W1973737539 creator A5022013143 @default.
- W1973737539 date "2009-02-01" @default.
- W1973737539 modified "2023-09-26" @default.
- W1973737539 title "Chromophore Isomerization Has Large Effects On The Residual Structure Of The Fully Unfolded State Of The Blue Light Receptor Photoactive Yellow Protein" @default.
- W1973737539 doi "https://doi.org/10.1016/j.bpj.2008.12.3728" @default.
- W1973737539 hasPublicationYear "2009" @default.
- W1973737539 type Work @default.
- W1973737539 sameAs 1973737539 @default.
- W1973737539 citedByCount "0" @default.
- W1973737539 crossrefType "journal-article" @default.
- W1973737539 hasAuthorship W1973737539A5008471776 @default.
- W1973737539 hasAuthorship W1973737539A5022013143 @default.
- W1973737539 hasBestOaLocation W19737375391 @default.
- W1973737539 hasConcept C119599485 @default.
- W1973737539 hasConcept C121332964 @default.
- W1973737539 hasConcept C121745418 @default.
- W1973737539 hasConcept C126661725 @default.
- W1973737539 hasConcept C127413603 @default.
- W1973737539 hasConcept C133571119 @default.
- W1973737539 hasConcept C13965031 @default.
- W1973737539 hasConcept C161790260 @default.
- W1973737539 hasConcept C166014724 @default.
- W1973737539 hasConcept C175188612 @default.
- W1973737539 hasConcept C178790620 @default.
- W1973737539 hasConcept C185592680 @default.
- W1973737539 hasConcept C192468462 @default.
- W1973737539 hasConcept C19472624 @default.
- W1973737539 hasConcept C204328495 @default.
- W1973737539 hasConcept C2776545253 @default.
- W1973737539 hasConcept C2776923230 @default.
- W1973737539 hasConcept C55493867 @default.
- W1973737539 hasConcept C62520636 @default.
- W1973737539 hasConcept C75473681 @default.
- W1973737539 hasConcept C8010536 @default.
- W1973737539 hasConcept C85311670 @default.
- W1973737539 hasConcept C91881484 @default.
- W1973737539 hasConceptScore W1973737539C119599485 @default.
- W1973737539 hasConceptScore W1973737539C121332964 @default.
- W1973737539 hasConceptScore W1973737539C121745418 @default.
- W1973737539 hasConceptScore W1973737539C126661725 @default.
- W1973737539 hasConceptScore W1973737539C127413603 @default.
- W1973737539 hasConceptScore W1973737539C133571119 @default.
- W1973737539 hasConceptScore W1973737539C13965031 @default.
- W1973737539 hasConceptScore W1973737539C161790260 @default.
- W1973737539 hasConceptScore W1973737539C166014724 @default.
- W1973737539 hasConceptScore W1973737539C175188612 @default.
- W1973737539 hasConceptScore W1973737539C178790620 @default.
- W1973737539 hasConceptScore W1973737539C185592680 @default.
- W1973737539 hasConceptScore W1973737539C192468462 @default.
- W1973737539 hasConceptScore W1973737539C19472624 @default.
- W1973737539 hasConceptScore W1973737539C204328495 @default.
- W1973737539 hasConceptScore W1973737539C2776545253 @default.
- W1973737539 hasConceptScore W1973737539C2776923230 @default.
- W1973737539 hasConceptScore W1973737539C55493867 @default.
- W1973737539 hasConceptScore W1973737539C62520636 @default.
- W1973737539 hasConceptScore W1973737539C75473681 @default.
- W1973737539 hasConceptScore W1973737539C8010536 @default.
- W1973737539 hasConceptScore W1973737539C85311670 @default.
- W1973737539 hasConceptScore W1973737539C91881484 @default.
- W1973737539 hasIssue "3" @default.
- W1973737539 hasLocation W19737375391 @default.
- W1973737539 hasOpenAccess W1973737539 @default.
- W1973737539 hasPrimaryLocation W19737375391 @default.
- W1973737539 hasRelatedWork W1973737539 @default.
- W1973737539 hasRelatedWork W1982555027 @default.
- W1973737539 hasRelatedWork W1988120860 @default.
- W1973737539 hasRelatedWork W2024698943 @default.
- W1973737539 hasRelatedWork W2034516179 @default.
- W1973737539 hasRelatedWork W2050674574 @default.
- W1973737539 hasRelatedWork W2058629823 @default.
- W1973737539 hasRelatedWork W2094422470 @default.
- W1973737539 hasRelatedWork W2465858892 @default.
- W1973737539 hasRelatedWork W2469117579 @default.
- W1973737539 hasVolume "96" @default.
- W1973737539 isParatext "false" @default.
- W1973737539 isRetracted "false" @default.
- W1973737539 magId "1973737539" @default.
- W1973737539 workType "article" @default.