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Description
| - The amyloid fibril of bovine insulin and its renaturing intermediates were studied by using Raman optical activity (ROA). In the spectrum of the amyloid, the sharp +/- ROA couplet of amide I band characteristic of the beta-sheet-rich proteins was observed, together with a sharp peak at 1271 cm(-1) characteristic of a turn structure. The shoulder ROA peak of the native insulin at similar to 1340 cm(-1), which was assigned to the hydrated alpha-helix, was not observed in the amyloid, suggesting that the hydrated alpha-helix was converted to the parallel beta-sheet structure in the amyloid. Recovery of the amyloid to the native state was also monitored by ROA. The intermediate states showed distinct features from the amyloid or native ones. The intermediates did not show a characteristic ROA peak of the poly(L-proline) II helix at similar to 1318 cm(-1). The hydrated alpha-helix ROA peak was not recovered in the intermediate states. In a process of the amyloid formation, at first the hydrated alpha-helix of the native insulin is converted to a specific partially unfolded structure, and then, it was converted to the parallel beta-sheet structure with many turns.
- The amyloid fibril of bovine insulin and its renaturing intermediates were studied by using Raman optical activity (ROA). In the spectrum of the amyloid, the sharp +/- ROA couplet of amide I band characteristic of the beta-sheet-rich proteins was observed, together with a sharp peak at 1271 cm(-1) characteristic of a turn structure. The shoulder ROA peak of the native insulin at similar to 1340 cm(-1), which was assigned to the hydrated alpha-helix, was not observed in the amyloid, suggesting that the hydrated alpha-helix was converted to the parallel beta-sheet structure in the amyloid. Recovery of the amyloid to the native state was also monitored by ROA. The intermediate states showed distinct features from the amyloid or native ones. The intermediates did not show a characteristic ROA peak of the poly(L-proline) II helix at similar to 1318 cm(-1). The hydrated alpha-helix ROA peak was not recovered in the intermediate states. In a process of the amyloid formation, at first the hydrated alpha-helix of the native insulin is converted to a specific partially unfolded structure, and then, it was converted to the parallel beta-sheet structure with many turns. (en)
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Title
| - Raman optical activity study on insulin amyloid- and prefibril intermediate
- Raman optical activity study on insulin amyloid- and prefibril intermediate (en)
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skos:prefLabel
| - Raman optical activity study on insulin amyloid- and prefibril intermediate
- Raman optical activity study on insulin amyloid- and prefibril intermediate (en)
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skos:notation
| - RIV/61388963:_____/12:00377069!RIV13-AV0-61388963
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http://linked.open...avai/riv/aktivita
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http://linked.open...avai/riv/aktivity
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http://linked.open...iv/cisloPeriodika
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http://linked.open...vai/riv/dodaniDat
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http://linked.open...aciTvurceVysledku
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http://linked.open.../riv/druhVysledku
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http://linked.open...iv/duvernostUdaju
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http://linked.open...titaPredkladatele
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http://linked.open...dnocenehoVysledku
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http://linked.open...ai/riv/idVysledku
| - RIV/61388963:_____/12:00377069
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http://linked.open...riv/jazykVysledku
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http://linked.open.../riv/klicovaSlova
| - raman optical activity; amyloid; fibril; intermediate; insulin (en)
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http://linked.open.../riv/klicoveSlovo
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http://linked.open...odStatuVydavatele
| - US - Spojené státy americké
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http://linked.open...ontrolniKodProRIV
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http://linked.open...i/riv/nazevZdroje
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http://linked.open...in/vavai/riv/obor
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http://linked.open...ichTvurcuVysledku
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http://linked.open...cetTvurcuVysledku
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http://linked.open...UplatneniVysledku
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http://linked.open...v/svazekPeriodika
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http://linked.open...iv/tvurceVysledku
| - Watarai, H.
- Yamamoto, Shigeki
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http://linked.open...ain/vavai/riv/wos
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http://linked.open...n/vavai/riv/zamer
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issn
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number of pages
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http://bibframe.org/vocab/doi
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