Solvated States of Poly-L-alanine alpha-Helix Explored by Raman Optical Activity

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F14%3A00429543" target="_blank" >RIV/61388963:_____/14:00429543 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1021/jp500794s" target="_blank" >http://dx.doi.org/10.1021/jp500794s</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/jp500794s" target="_blank" >10.1021/jp500794s</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Solvated States of Poly-L-alanine alpha-Helix Explored by Raman Optical Activity

Popis výsledku v původním jazyce

Raman optical activity (ROA) reveals surprising details of the secondary structure of polypeptides and proteins in solution phase. Yet specific spectral features, such as in the extended amide III region of hydrated alpha-helix, did not seem explicable by the generally accepted sensitivity of ROA to the local conformation. This is reconciled in the present study by simulations of ROA spectra for model alpha-helical structures. Two positive ROA peaks often observed at around 1340 and 1300 cm(-1) for polypeptides and proteins have been assigned to two types of solvated alpha-helices; one is stable in hydrophilic environment where amide groups make hydrogen bonds to solvent molecules or polar side chains (similar to 1340 cm(-1)), and the other is supported by a hydrophobic environment without the possibility of external hydrogen bonds (similar to 1300 cm(-1)). For poly-L-alanine (PLA), regarded as a good model of a-helical structure, the experimentally observed relative intensity ratio of

Název v anglickém jazyce

Solvated States of Poly-L-alanine alpha-Helix Explored by Raman Optical Activity

Popis výsledku anglicky

Raman optical activity (ROA) reveals surprising details of the secondary structure of polypeptides and proteins in solution phase. Yet specific spectral features, such as in the extended amide III region of hydrated alpha-helix, did not seem explicable by the generally accepted sensitivity of ROA to the local conformation. This is reconciled in the present study by simulations of ROA spectra for model alpha-helical structures. Two positive ROA peaks often observed at around 1340 and 1300 cm(-1) for polypeptides and proteins have been assigned to two types of solvated alpha-helices; one is stable in hydrophilic environment where amide groups make hydrogen bonds to solvent molecules or polar side chains (similar to 1340 cm(-1)), and the other is supported by a hydrophobic environment without the possibility of external hydrogen bonds (similar to 1300 cm(-1)). For poly-L-alanine (PLA), regarded as a good model of a-helical structure, the experimentally observed relative intensity ratio of

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

<a href="/cs/project/GAP208%2F11%2F0105" target="_blank" >GAP208/11/0105: Rozšíření metod vibrační optické aktivity pro oblast biomolekul</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2014

Kód důvěrnosti údajů

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

Název periodika

Journal of Physical Chemistry A

ISSN

1089-5639

e-ISSN

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Svazek periodika

118

Číslo periodika v rámci svazku

20

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

8

Strana od-do

3655-3662

Kód UT WoS článku

000336510500013

EID výsledku v databázi Scopus

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