Matches in SemOpenAlex for { <https://semopenalex.org/work/W2062080188> ?p ?o ?g. }
Showing items 1 to 97 of
97
with 100 items per page.
- W2062080188 endingPage "9957" @default.
- W2062080188 startingPage "9951" @default.
- W2062080188 abstract "Twelve sequential single cysteine mutants of alphaA-crystallin extending between amino acids Y109 and L120 were prepared and reacted with a sulfhydryl specific spin label in order to investigate the role of this sequence in the assembly of the alphaA-crystallin quaternary structure and its chaperone-like function. The sequence is located in the region of highest homology in the alpha-crystallin domain, a stretch of 100 amino acids conserved among lens alpha-crystallins and small heat-shock proteins (sHSPs). Analysis of the solvent accessibility and mobility of the attached nitroxides reveals that the sequence, as a whole, is relatively sequestered from the aqueous solvent. Furthermore, as teh nitroxide is scanned across the sequence, both mobility and accessibility vary with a periodicity of 2, demonstrating that the backbone conformation is that of a beta-strand. Once face of the strand, containing the highly conserved residues R112 and R116, is buried with virtually no accessibility to the aqueous solvent. Equivalent strands from different subunits are in close spatial proximity, as inferred from spin-spin interactions between identical residues along the strand. Taken together, our results are consistent with the hypothesis that the alpha-crystallin domain is a building block of the alpha-crystallins quaternary structure and suggest that the charge conservation observed in the alpha-crystallins evolution might be important for the assembly of the oligomer. This work reports the first use of SDSL to identify a beta-strand in an unknown structure and demonstrates the feasibility of using this technique to investigate the oligomeric structure of the alpha-crystallins and sHSPs." @default.
- W2062080188 created "2016-06-24" @default.
- W2062080188 creator A5059881003 @default.
- W2062080188 creator A5074787698 @default.
- W2062080188 creator A5079315150 @default.
- W2062080188 date "1997-08-01" @default.
- W2062080188 modified "2023-10-09" @default.
- W2062080188 title "Structure and Function of the Conserved Domain in αA-Crystallin. Site-Directed Spin Labeling Identifies a β-Strand Located near a Subunit Interface" @default.
- W2062080188 cites W1508885706 @default.
- W2062080188 cites W151404467 @default.
- W2062080188 cites W1671787304 @default.
- W2062080188 cites W1963687863 @default.
- W2062080188 cites W2011845231 @default.
- W2062080188 cites W2020332937 @default.
- W2062080188 cites W2025388082 @default.
- W2062080188 cites W2033597620 @default.
- W2062080188 cites W2045683458 @default.
- W2062080188 cites W2086675715 @default.
- W2062080188 cites W2090785584 @default.
- W2062080188 cites W2093924477 @default.
- W2062080188 doi "https://doi.org/10.1021/bi9712347" @default.
- W2062080188 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9296605" @default.
- W2062080188 hasPublicationYear "1997" @default.
- W2062080188 type Work @default.
- W2062080188 sameAs 2062080188 @default.
- W2062080188 citedByCount "91" @default.
- W2062080188 countsByYear W20620801882012 @default.
- W2062080188 countsByYear W20620801882013 @default.
- W2062080188 countsByYear W20620801882014 @default.
- W2062080188 countsByYear W20620801882015 @default.
- W2062080188 countsByYear W20620801882016 @default.
- W2062080188 countsByYear W20620801882017 @default.
- W2062080188 countsByYear W20620801882018 @default.
- W2062080188 countsByYear W20620801882020 @default.
- W2062080188 countsByYear W20620801882023 @default.
- W2062080188 crossrefType "journal-article" @default.
- W2062080188 hasAuthorship W2062080188A5059881003 @default.
- W2062080188 hasAuthorship W2062080188A5074787698 @default.
- W2062080188 hasAuthorship W2062080188A5079315150 @default.
- W2062080188 hasConcept C104292427 @default.
- W2062080188 hasConcept C104317684 @default.
- W2062080188 hasConcept C12554922 @default.
- W2062080188 hasConcept C167625842 @default.
- W2062080188 hasConcept C177462420 @default.
- W2062080188 hasConcept C181199279 @default.
- W2062080188 hasConcept C185592680 @default.
- W2062080188 hasConcept C199216141 @default.
- W2062080188 hasConcept C2779201268 @default.
- W2062080188 hasConcept C41625074 @default.
- W2062080188 hasConcept C47701112 @default.
- W2062080188 hasConcept C515207424 @default.
- W2062080188 hasConcept C55493867 @default.
- W2062080188 hasConcept C71240020 @default.
- W2062080188 hasConcept C7263354 @default.
- W2062080188 hasConcept C7927669 @default.
- W2062080188 hasConcept C8010536 @default.
- W2062080188 hasConcept C86803240 @default.
- W2062080188 hasConceptScore W2062080188C104292427 @default.
- W2062080188 hasConceptScore W2062080188C104317684 @default.
- W2062080188 hasConceptScore W2062080188C12554922 @default.
- W2062080188 hasConceptScore W2062080188C167625842 @default.
- W2062080188 hasConceptScore W2062080188C177462420 @default.
- W2062080188 hasConceptScore W2062080188C181199279 @default.
- W2062080188 hasConceptScore W2062080188C185592680 @default.
- W2062080188 hasConceptScore W2062080188C199216141 @default.
- W2062080188 hasConceptScore W2062080188C2779201268 @default.
- W2062080188 hasConceptScore W2062080188C41625074 @default.
- W2062080188 hasConceptScore W2062080188C47701112 @default.
- W2062080188 hasConceptScore W2062080188C515207424 @default.
- W2062080188 hasConceptScore W2062080188C55493867 @default.
- W2062080188 hasConceptScore W2062080188C71240020 @default.
- W2062080188 hasConceptScore W2062080188C7263354 @default.
- W2062080188 hasConceptScore W2062080188C7927669 @default.
- W2062080188 hasConceptScore W2062080188C8010536 @default.
- W2062080188 hasConceptScore W2062080188C86803240 @default.
- W2062080188 hasIssue "33" @default.
- W2062080188 hasLocation W20620801881 @default.
- W2062080188 hasLocation W20620801882 @default.
- W2062080188 hasOpenAccess W2062080188 @default.
- W2062080188 hasPrimaryLocation W20620801881 @default.
- W2062080188 hasRelatedWork W1975889581 @default.
- W2062080188 hasRelatedWork W198328665 @default.
- W2062080188 hasRelatedWork W1985666157 @default.
- W2062080188 hasRelatedWork W2015059765 @default.
- W2062080188 hasRelatedWork W2041438710 @default.
- W2062080188 hasRelatedWork W2044690163 @default.
- W2062080188 hasRelatedWork W2161227450 @default.
- W2062080188 hasRelatedWork W2762966506 @default.
- W2062080188 hasRelatedWork W3108975412 @default.
- W2062080188 hasRelatedWork W3131413015 @default.
- W2062080188 hasVolume "36" @default.
- W2062080188 isParatext "false" @default.
- W2062080188 isRetracted "false" @default.
- W2062080188 magId "2062080188" @default.
- W2062080188 workType "article" @default.