Matches in SemOpenAlex for { <https://semopenalex.org/work/W2026515270> ?p ?o ?g. }
Showing items 1 to 79 of
79
with 100 items per page.
- W2026515270 endingPage "5633" @default.
- W2026515270 startingPage "5626" @default.
- W2026515270 abstract "The formation of closed icosahedral capsids from a single species of coat protein subunit requires that the subunits assume different conformations at different lattice positions. In the double-stranded DNA bacteriophage P22, formation of correctly dimensioned capsids is mediated by interaction between coat protein subunits and scaffolding protein. Raman spectroscopy has been employed to compare the conformations of coat protein subunits which have been polymerized to form capsids in the presence and absence of the of scaffolding protein display a Raman spectrum characterized by a broad amide I band centered at 1665 cm-1 with a discernible shoulder near 1653 cm-1, and a broad amide III profile centered at 1238 cm-1 but asymmetrically skewed to higher frequency. These spectral features indicate that the protein conformation in procapsid shells is rich in beta-sheet secondary structure but contains also a significant distribution of alpha-helix. When biologically active, purified subunits assemble in the absence of scaffolding protein, they form polydisperse multimers lacking the proper dimensions of procapsid closed shells. We designate these multimers as associated subunits (AS). The Raman spectrum of associated subunits indicates a narrower distribution of secondary structure. The associated subunits are characterized by a sharper and more intense Raman amide I band at 1666 cm-1, with no prominent amide I shoulder of lower frequency. An analogous narrowing of the Raman amide III profile is also observed for AS particles, with an accompanying shift of the amide III band center to 1235 cm-1.(ABSTRACT TRUNCATED AT 250 WORDS)" @default.
- W2026515270 created "2016-06-24" @default.
- W2026515270 creator A5002701325 @default.
- W2026515270 creator A5013482566 @default.
- W2026515270 creator A5058402118 @default.
- W2026515270 creator A5066254776 @default.
- W2026515270 creator A5076114463 @default.
- W2026515270 date "1990-06-01" @default.
- W2026515270 modified "2023-10-16" @default.
- W2026515270 title "Conformational states of the bacteriophage P22 capsid subunit in relation to self-assembly" @default.
- W2026515270 doi "https://doi.org/10.1021/bi00475a030" @default.
- W2026515270 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2386790" @default.
- W2026515270 hasPublicationYear "1990" @default.
- W2026515270 type Work @default.
- W2026515270 sameAs 2026515270 @default.
- W2026515270 citedByCount "27" @default.
- W2026515270 countsByYear W20265152702012 @default.
- W2026515270 countsByYear W20265152702013 @default.
- W2026515270 countsByYear W20265152702014 @default.
- W2026515270 crossrefType "journal-article" @default.
- W2026515270 hasAuthorship W2026515270A5002701325 @default.
- W2026515270 hasAuthorship W2026515270A5013482566 @default.
- W2026515270 hasAuthorship W2026515270A5058402118 @default.
- W2026515270 hasAuthorship W2026515270A5066254776 @default.
- W2026515270 hasAuthorship W2026515270A5076114463 @default.
- W2026515270 hasConcept C104292427 @default.
- W2026515270 hasConcept C104317684 @default.
- W2026515270 hasConcept C113709186 @default.
- W2026515270 hasConcept C120665830 @default.
- W2026515270 hasConcept C121332964 @default.
- W2026515270 hasConcept C12554922 @default.
- W2026515270 hasConcept C185592680 @default.
- W2026515270 hasConcept C202878990 @default.
- W2026515270 hasConcept C2776441376 @default.
- W2026515270 hasConcept C2778439535 @default.
- W2026515270 hasConcept C40003534 @default.
- W2026515270 hasConcept C547475151 @default.
- W2026515270 hasConcept C55493867 @default.
- W2026515270 hasConcept C62614982 @default.
- W2026515270 hasConcept C8010536 @default.
- W2026515270 hasConcept C86803240 @default.
- W2026515270 hasConceptScore W2026515270C104292427 @default.
- W2026515270 hasConceptScore W2026515270C104317684 @default.
- W2026515270 hasConceptScore W2026515270C113709186 @default.
- W2026515270 hasConceptScore W2026515270C120665830 @default.
- W2026515270 hasConceptScore W2026515270C121332964 @default.
- W2026515270 hasConceptScore W2026515270C12554922 @default.
- W2026515270 hasConceptScore W2026515270C185592680 @default.
- W2026515270 hasConceptScore W2026515270C202878990 @default.
- W2026515270 hasConceptScore W2026515270C2776441376 @default.
- W2026515270 hasConceptScore W2026515270C2778439535 @default.
- W2026515270 hasConceptScore W2026515270C40003534 @default.
- W2026515270 hasConceptScore W2026515270C547475151 @default.
- W2026515270 hasConceptScore W2026515270C55493867 @default.
- W2026515270 hasConceptScore W2026515270C62614982 @default.
- W2026515270 hasConceptScore W2026515270C8010536 @default.
- W2026515270 hasConceptScore W2026515270C86803240 @default.
- W2026515270 hasIssue "23" @default.
- W2026515270 hasLocation W20265152701 @default.
- W2026515270 hasLocation W20265152702 @default.
- W2026515270 hasOpenAccess W2026515270 @default.
- W2026515270 hasPrimaryLocation W20265152701 @default.
- W2026515270 hasRelatedWork W1984134553 @default.
- W2026515270 hasRelatedWork W1985651475 @default.
- W2026515270 hasRelatedWork W1998773331 @default.
- W2026515270 hasRelatedWork W2058590671 @default.
- W2026515270 hasRelatedWork W2101895029 @default.
- W2026515270 hasRelatedWork W2169259183 @default.
- W2026515270 hasRelatedWork W2754702332 @default.
- W2026515270 hasRelatedWork W2916783191 @default.
- W2026515270 hasRelatedWork W2926505747 @default.
- W2026515270 hasRelatedWork W4210536547 @default.
- W2026515270 hasVolume "29" @default.
- W2026515270 isParatext "false" @default.
- W2026515270 isRetracted "false" @default.
- W2026515270 magId "2026515270" @default.
- W2026515270 workType "article" @default.