Differences in conformational behavior of amyloid beta in solvent with different ionic strength

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F09%3A00029983" target="_blank" >RIV/00216224:14310/09:00029983 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Differences in conformational behavior of amyloid beta in solvent with different ionic strength

Popis výsledku v původním jazyce

INTRODUCTION Amyloid beta-peptide (Abeta) is the major component of plaques found in the brains of Alzheimers patients. Among its two predominate forms - Abeta(1-40) and Abeta(1-42), the latter possesses stronger aggregation and deposition propensity than the former. To explore the conformational preference of Abeta(1-42) in solvent with different ionic strength, molecular dynamics (MD) simulations were performed. METHODS The human Abeta(1-42) structure presented in PDB database (code 1Z0Q) was used asstarting point for MD simulations. The rat structure was prepared from human by mutation of 3 residues using Modeller software. The input structures were solvated by program SOLVATE and sodium and chloride ions in different concentrations were added to the system. For each system, 50 ns long trajectory was run and stability of the secondary structures of the protein was investigated.

Název v anglickém jazyce

Differences in conformational behavior of amyloid beta in solvent with different ionic strength

Popis výsledku anglicky

INTRODUCTION Amyloid beta-peptide (Abeta) is the major component of plaques found in the brains of Alzheimers patients. Among its two predominate forms - Abeta(1-40) and Abeta(1-42), the latter possesses stronger aggregation and deposition propensity than the former. To explore the conformational preference of Abeta(1-42) in solvent with different ionic strength, molecular dynamics (MD) simulations were performed. METHODS The human Abeta(1-42) structure presented in PDB database (code 1Z0Q) was used asstarting point for MD simulations. The rat structure was prepared from human by mutation of 3 residues using Modeller software. The input structures were solvated by program SOLVATE and sodium and chloride ions in different concentrations were added to the system. For each system, 50 ns long trajectory was run and stability of the secondary structures of the protein was investigated.

Druh

D - Stať ve sborníku

CEP obor

CF - Fyzikální chemie a teoretická chemie

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>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2009

Kód důvěrnosti údajů

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

Název statě ve sborníku

34th Congress of the Federation-of-European-Biochemical-Societies

ISBN

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ISSN

1742-464X

e-ISSN

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Počet stran výsledku

1

Strana od-do

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Název nakladatele

Wiley-Blackwell

Místo vydání

Oxford

Místo konání akce

Praha

Datum konání akce

1. 1. 2009

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

000267069900418