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DC Field | Value | Language |
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dc.citation.endPage | 7725 | - |
dc.citation.number | 22 | - |
dc.citation.startPage | 7720 | - |
dc.citation.title | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OFAMERICA | - |
dc.citation.volume | 105 | - |
dc.contributor.author | Kim, Yung Sam | - |
dc.contributor.author | Liu, Liu | - |
dc.contributor.author | Axelsen, Paul H. | - |
dc.contributor.author | Hochstrasser, Robin M. | - |
dc.date.accessioned | 2023-12-22T08:39:25Z | - |
dc.date.available | 2023-12-22T08:39:25Z | - |
dc.date.created | 2014-11-14 | - |
dc.date.issued | 2008-06 | - |
dc.description.abstract | The 2D IR spectra of the amide-I vibrations of amyloid fibrils from Aβ40 were obtained. The matured fibrils formed from strands having isotopic substitution by 13C=18O at Gly-38, Gly-33, Gly-29, or Ala-21 show vibrational exciton spectra having reduced dimensionality. Indeed, linear chain excitons of amide units are seen, for which the interamide vibrational coupling is measured in fibrils grown from 50% and 5% mixtures of labeled and unlabeled strands. The data prove that the 1D excitons are formed from parallel in-register sheets. The coupling constants show that for each of the indicated residues the amide carbonyls in the chains are separated by 0.5 ± 0.05 nm. The isotope replacement of Gly-25 does not reveal linear excitons, consistent with the region of the strand having a different structure distribution. The vibrational frequencies of the amide-I modes, freed from effects of amide vibrational excitation exchange by 5% dilution experiments, point to there being a component of an electric field along the fibril axis that increases through the sequence Gly-38, Gly-33, Gly-29. The field is dominated by side chains of neighboring residues. | - |
dc.identifier.bibliographicCitation | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OFAMERICA, v.105, no.22, pp.7720 - 7725 | - |
dc.identifier.doi | 10.1073/pnas.0802993105 | - |
dc.identifier.issn | 0027-8424 | - |
dc.identifier.scopusid | 2-s2.0-45549085028 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/8938 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=45549085028 | - |
dc.identifier.wosid | 000256648600019 | - |
dc.language | 영어 | - |
dc.publisher | NATL ACAD SCIENCES | - |
dc.title | Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from A beta 40 | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordAuthor | beta-amyloid 40 | - |
dc.subject.keywordAuthor | exciton | - |
dc.subject.keywordAuthor | two-dimensional infrared spectroscopy | - |
dc.subject.keywordPlus | BETA-SHEET STRUCTURE | - |
dc.subject.keywordPlus | 2D IR SPECTROSCOPY | - |
dc.subject.keywordPlus | X-RAY-DIFFRACTION | - |
dc.subject.keywordPlus | SOLID-STATE NMR |
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dc.subject.keywordPlus | EXPERIMENTAL CONSTRAINTS | - |
dc.subject.keywordPlus | ALZHEIMER-DISEASE | - |
dc.subject.keywordPlus | FRENKEL EXCITONS | - |
dc.subject.keywordPlus | PEPTIDE | - |
dc.subject.keywordPlus | PARALLEL | - |
dc.subject.keywordPlus | DYNAMICS | - |
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