FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2049876291> ?p ?o ?g. }

• W2049876291 endingPage "1288" @default.
• W2049876291 startingPage "1275" @default.
• W2049876291 abstract "The effects of lacking a specific disulfide bridge on the transition state in folding were examined in order to explore the folding-unfolding mechanism of lysozyme. Four species of three-disulfide variant of hen lysozyme (3SS-lysozyme) were prepared by replacing two Cys residues with Ala or Ser: C6S/C127A, C30A/C115A, C64A/C80A and C76A/C94A. The recombinant hen lysozyme was studied as the standard reference containing four authentic disulfide bridges and the extra N-terminal Met: the recombinant hen lysozyme containing the extra N-terminal. Folding rates were measured by monitoring the change in fluorescence intensity associated with tri-N-acetyl-d-glucosamine binding to the active site of refolded lysozyme. It was confirmed that the folding rate of the recombinant hen lysozyme containing the extra N-terminal was the same as that of wild-type lysozyme, and that the folding rate was little affected by the presence of tri-N-acetyl-d-glucosamine (triNAG). The folding rate of C64A/C80A was found to be the fastest and almost the same as that of the recombinant hen lysozyme containing the extra N-terminal, and that of C30A/C115A the second, and that of C6S/C127A the third. The folding rate of C76A/C94A was particularly slow. On the other hand, the unfolding rates which were measured in the presence of triNAG showed the dependence on the concentration of triNAG. The intrinsic unfolding rate in the absence of triNAG was determined by extrapolation. Also in the unfolding rate, C76A/C94A was markedly slower than the others. It was found from the analysis of binding constants of triNAG to C64A/C80A during the unfolding process that the active site of C64A/C80A partly unfolds already prior to the unfolding transition. On the basis of these kinetic data, we suggest that C64A/C80A folding transition can occur with leaving the loop region around SS3 (C64-C80) flexible, while cross-linking by SS4 (C76-C94) is important for the promotion of folding, because it is an indispensable constraint on the way towards the folding transition state." @default.
• W2049876291 created "2016-06-24" @default.
• W2049876291 creator A5006930810 @default.
• W2049876291 creator A5039235243 @default.
• W2049876291 creator A5039623511 @default.
• W2049876291 creator A5044942161 @default.
• W2049876291 creator A5080969987 @default.
• W2049876291 creator A5085539789 @default.
• W2049876291 creator A5090022183 @default.
• W2049876291 creator A5090902825 @default.
• W2049876291 date "2000-02-01" @default.
• W2049876291 modified "2023-09-26" @default.
• W2049876291 title "The transition state in the folding-unfolding reaction of four species of three-disulfide variant of hen lysozyme: the role of each disulfide bridge" @default.
• W2049876291 cites W1512176015 @default.
• W2049876291 cites W1593374398 @default.
• W2049876291 cites W1964118138 @default.
• W2049876291 cites W1979038840 @default.
• W2049876291 cites W1983953936 @default.
• W2049876291 cites W1992230954 @default.
• W2049876291 cites W1993703672 @default.
• W2049876291 cites W2005865331 @default.
• W2049876291 cites W2008585649 @default.
• W2049876291 cites W2020800669 @default.
• W2049876291 cites W2023368588 @default.
• W2049876291 cites W2029871341 @default.
• W2049876291 cites W2030412899 @default.
• W2049876291 cites W2046685910 @default.
• W2049876291 cites W2051302860 @default.
• W2049876291 cites W2075454119 @default.
• W2049876291 cites W2078916999 @default.
• W2049876291 cites W2085479332 @default.
• W2049876291 cites W2088397672 @default.
• W2049876291 cites W2094539955 @default.
• W2049876291 cites W2107276905 @default.
• W2049876291 cites W2130681711 @default.
• W2049876291 cites W2134878199 @default.
• W2049876291 doi "https://doi.org/10.1006/jmbi.1999.3442" @default.
• W2049876291 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10653703" @default.
• W2049876291 hasPublicationYear "2000" @default.
• W2049876291 type Work @default.
• W2049876291 sameAs 2049876291 @default.
• W2049876291 citedByCount "44" @default.
• W2049876291 countsByYear W20498762912012 @default.
• W2049876291 countsByYear W20498762912013 @default.
• W2049876291 countsByYear W20498762912014 @default.
• W2049876291 countsByYear W20498762912017 @default.
• W2049876291 countsByYear W20498762912018 @default.
• W2049876291 countsByYear W20498762912020 @default.
• W2049876291 countsByYear W20498762912021 @default.
• W2049876291 crossrefType "journal-article" @default.
• W2049876291 hasAuthorship W2049876291A5006930810 @default.
• W2049876291 hasAuthorship W2049876291A5039235243 @default.
• W2049876291 hasAuthorship W2049876291A5039623511 @default.
• W2049876291 hasAuthorship W2049876291A5044942161 @default.
• W2049876291 hasAuthorship W2049876291A5080969987 @default.
• W2049876291 hasAuthorship W2049876291A5085539789 @default.
• W2049876291 hasAuthorship W2049876291A5090022183 @default.
• W2049876291 hasAuthorship W2049876291A5090902825 @default.
• W2049876291 hasConcept C119599485 @default.
• W2049876291 hasConcept C121332964 @default.
• W2049876291 hasConcept C12554922 @default.
• W2049876291 hasConcept C127413603 @default.
• W2049876291 hasConcept C148898269 @default.
• W2049876291 hasConcept C185592680 @default.
• W2049876291 hasConcept C204328495 @default.
• W2049876291 hasConcept C27256138 @default.
• W2049876291 hasConcept C2776545253 @default.
• W2049876291 hasConcept C2776966407 @default.
• W2049876291 hasConcept C55493867 @default.
• W2049876291 hasConcept C62520636 @default.
• W2049876291 hasConcept C8010536 @default.
• W2049876291 hasConcept C86803240 @default.
• W2049876291 hasConceptScore W2049876291C119599485 @default.
• W2049876291 hasConceptScore W2049876291C121332964 @default.
• W2049876291 hasConceptScore W2049876291C12554922 @default.
• W2049876291 hasConceptScore W2049876291C127413603 @default.
• W2049876291 hasConceptScore W2049876291C148898269 @default.
• W2049876291 hasConceptScore W2049876291C185592680 @default.
• W2049876291 hasConceptScore W2049876291C204328495 @default.
• W2049876291 hasConceptScore W2049876291C27256138 @default.
• W2049876291 hasConceptScore W2049876291C2776545253 @default.
• W2049876291 hasConceptScore W2049876291C2776966407 @default.
• W2049876291 hasConceptScore W2049876291C55493867 @default.
• W2049876291 hasConceptScore W2049876291C62520636 @default.
• W2049876291 hasConceptScore W2049876291C8010536 @default.
• W2049876291 hasConceptScore W2049876291C86803240 @default.
• W2049876291 hasIssue "5" @default.
• W2049876291 hasLocation W20498762911 @default.
• W2049876291 hasLocation W20498762912 @default.
• W2049876291 hasOpenAccess W2049876291 @default.
• W2049876291 hasPrimaryLocation W20498762911 @default.
• W2049876291 hasRelatedWork W1527420168 @default.
• W2049876291 hasRelatedWork W1544937449 @default.
• W2049876291 hasRelatedWork W1972973622 @default.
• W2049876291 hasRelatedWork W2065971324 @default.
• W2049876291 hasRelatedWork W2081163211 @default.
• W2049876291 hasRelatedWork W2112763744 @default.
• W2049876291 hasRelatedWork W2315657566 @default.

• next