Raman optical activity study on insulin amyloid- and prefibril intermediate

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F12%3A00377069" target="_blank" >RIV/61388963:_____/12:00377069 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1002/chir.21029" target="_blank" >http://dx.doi.org/10.1002/chir.21029</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/chir.21029" target="_blank" >10.1002/chir.21029</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Raman optical activity study on insulin amyloid- and prefibril intermediate

Popis výsledku v původním jazyce

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 hydr

Název v anglickém jazyce

Raman optical activity study on insulin amyloid- and prefibril intermediate

Popis výsledku anglicky

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 hydr

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CF - Fyzikální chemie a teoretická chemie

OECD FORD obor

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Projekt

—

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2012

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Chirality

ISSN

0899-0042

e-ISSN

—

Svazek periodika

24

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

7

Strana od-do

97-103

Kód UT WoS článku

000298873000001

EID výsledku v databázi Scopus

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