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DC Field | Value | Language |
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dc.citation.endPage | 6619 | - |
dc.citation.number | 16 | - |
dc.citation.startPage | 6614 | - |
dc.citation.title | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | - |
dc.citation.volume | 106 | - |
dc.contributor.author | Shim, Sang-Hee | - |
dc.contributor.author | Gupta, Ruchi | - |
dc.contributor.author | Ling, Yun L. | - |
dc.contributor.author | Strasfeld, David B. | - |
dc.contributor.author | Raleigh, Daniel P. | - |
dc.contributor.author | Zanni, Martin T. | - |
dc.date.accessioned | 2023-12-22T08:07:51Z | - |
dc.date.available | 2023-12-22T08:07:51Z | - |
dc.date.created | 2014-10-13 | - |
dc.date.issued | 2009-04 | - |
dc.description.abstract | There is considerable interest in uncovering the pathway of amyloid formation because the toxic properties of amyloid likely stems from prefibril intermediates and not the fully formed fibrils. Using a recently invented method of collecting 2-dimensional infrared spectra and site-specific isotope labeling, we have measured the development of secondary structures for 6 residues during the aggregation process of the 37-residue polypeptide associated with type 2 diabetes, the human islet amyloid polypeptide (hIAPP). By monitoring the kinetics at 6 different labeled sites, we find that the peptides initially develop well-ordered structure in the region of the chain that is close to the ordered loop of the fibrils, followed by formation of the 2 parallel β-sheets with the N-terminal β-sheet likely forming before the C-terminal sheet. This experimental approach provides a detailed view of the aggregation pathway of hIAPP fibril formation as well as a general methodology for studying other amyloid forming proteins without the use of structure-perturbing labels. | - |
dc.identifier.bibliographicCitation | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.106, no.16, pp.6614 - 6619 | - |
dc.identifier.doi | 10.1073/pnas.0805957106 | - |
dc.identifier.issn | 0027-8424 | - |
dc.identifier.scopusid | 2-s2.0-66149084447 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/7150 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=66149084447 | - |
dc.identifier.wosid | 000265506800036 | - |
dc.language | 영어 | - |
dc.publisher | NATL ACAD SCIENCES | - |
dc.title | Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordAuthor | aggregation | - |
dc.subject.keywordAuthor | amylin | - |
dc.subject.keywordAuthor | fibers | - |
dc.subject.keywordAuthor | human islet amyloid polypeptide | - |
dc.subject.keywordAuthor | nucleation | - |
dc.subject.keywordPlus | FIBRIL FORMATION | - |
dc.subject.keywordPlus | BETA-HAIRPIN | - |
dc.subject.keywordPlus | POLYPEPTIDE | - |
dc.subject.keywordPlus | AMYLIN | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | FIBRILLOGENESIS | - |
dc.subject.keywordPlus | NUCLEATION | - |
dc.subject.keywordPlus | INHIBITOR | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordPlus | MEMBRANE | - |
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