Tracking of the Polyproline Folding by Density Functional Computations and Raman Optical Activity Spectra

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11320%2F11%3A10105441" target="_blank" >RIV/00216208:11320/11:10105441 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388963:_____/11:00369957

Výsledek na webu

<a href="http://dx.doi.org/10.1021/jp207706p" target="_blank" >http://dx.doi.org/10.1021/jp207706p</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/jp207706p" target="_blank" >10.1021/jp207706p</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Tracking of the Polyproline Folding by Density Functional Computations and Raman Optical Activity Spectra

Popis výsledku v původním jazyce

Polyprolines offer many opportunities to study factors influencing peptide and protein folding and structure. Longer chains can adopt two well-defined forms (PPI and PPII), but shorter peptides are quite flexible. To understand in detail the dependence of the secondary structure on the length and the interplay between the side chain and main chain conformation, zwitterionic (Pro)(N) models (with N = 2, 3, 4, 6, 9, 12 and longer inhomogeneous chains) were studied by a combination of the Raman and Raman optical activity (ROA) spectroscopy with the density functional theory (DFT). Potential surfaces were systematically explored for the shorter oligoprolines, and Boltzmann conformational ratios were obtained both for the main chain and the proline ring puckering. The predictions were verified by comparison of the experimental and simulated ROA spectra. The conformer ratios extracted from a decomposition of the experimental ROA into scaled computed spectra well reproduced Boltzmann populati

Název v anglickém jazyce

Tracking of the Polyproline Folding by Density Functional Computations and Raman Optical Activity Spectra

Popis výsledku anglicky

Polyprolines offer many opportunities to study factors influencing peptide and protein folding and structure. Longer chains can adopt two well-defined forms (PPI and PPII), but shorter peptides are quite flexible. To understand in detail the dependence of the secondary structure on the length and the interplay between the side chain and main chain conformation, zwitterionic (Pro)(N) models (with N = 2, 3, 4, 6, 9, 12 and longer inhomogeneous chains) were studied by a combination of the Raman and Raman optical activity (ROA) spectroscopy with the density functional theory (DFT). Potential surfaces were systematically explored for the shorter oligoprolines, and Boltzmann conformational ratios were obtained both for the main chain and the proline ring puckering. The predictions were verified by comparison of the experimental and simulated ROA spectra. The conformer ratios extracted from a decomposition of the experimental ROA into scaled computed spectra well reproduced Boltzmann populati

Druh

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

CEP obor

BO - Biofyzika

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2011

Kód důvěrnosti údajů

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

Název periodika

Journal of Physical Chemistry B

ISSN

1520-6106

e-ISSN

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Svazek periodika

115

Číslo periodika v rámci svazku

50

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

11

Strana od-do

15079-15089

Kód UT WoS článku

000297947500019

EID výsledku v databázi Scopus

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