LECTIN ? CARBOHYDRATE INTERACTIONS DRIVEN BY DISPERSION

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F13%3A00072705" target="_blank" >RIV/00216224:14740/13:00072705 - 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

LECTIN ? CARBOHYDRATE INTERACTIONS DRIVEN BY DISPERSION

Popis výsledku v původním jazyce

There are several ways how saccharides may interact with their receptors (e.g. classical hydrogen bonds, through metal ions as Ca(II)). The CH-pi interactions that occur between carbohydrates and aromatic amino-acids are also strongly involved in carbohydrate-recognition process. The strength and importance of the CH-pi carbohydrate-aromatic interaction is recently under heavy discussion among biomolecular scientists. Some of a recognition processes are performed by proteins called lectins, which are able to bind saccharides in a very specific way. In case of the RSL lectin, we have attempted for the first time to quantify how the CH/pi interaction contributes to an overall carbohydrate - protein interaction. We have used an experimental approach, creating single and double point mutants, combined with high level computational methods. Experimentally measured binding affinities were compared with computed carbohydrate-aromatic acid residue interaction energies.

Název v anglickém jazyce

LECTIN ? CARBOHYDRATE INTERACTIONS DRIVEN BY DISPERSION

Popis výsledku anglicky

There are several ways how saccharides may interact with their receptors (e.g. classical hydrogen bonds, through metal ions as Ca(II)). The CH-pi interactions that occur between carbohydrates and aromatic amino-acids are also strongly involved in carbohydrate-recognition process. The strength and importance of the CH-pi carbohydrate-aromatic interaction is recently under heavy discussion among biomolecular scientists. Some of a recognition processes are performed by proteins called lectins, which are able to bind saccharides in a very specific way. In case of the RSL lectin, we have attempted for the first time to quantify how the CH/pi interaction contributes to an overall carbohydrate - protein interaction. We have used an experimental approach, creating single and double point mutants, combined with high level computational methods. Experimentally measured binding affinities were compared with computed carbohydrate-aromatic acid residue interaction energies.

Druh

O - Ostatní výsledky

CEP obor

CF - Fyzikální chemie a teoretická chemie

OECD FORD obor

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Projekt

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Návaznosti

R - Projekt Ramcoveho programu EK

Rok uplatnění

2013

Kód důvěrnosti údajů

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