Studies of mutant lectin binding behaviour by microcalorimetry
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F14%3A00077914" target="_blank" >RIV/00216224:14310/14:00077914 - isvavai.cz</a>
Výsledek na webu
—
DOI - Digital Object Identifier
—
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Studies of mutant lectin binding behaviour by microcalorimetry
Popis výsledku v původním jazyce
Bacterial lectins help pathogens in adhesion to sugar moieties presented on the host cell surface. Therefore, lectins from pathogenic bacteria and their adhesion modes are the subject of intense study. On the other hand, understanding of the basic principles of the lectin-carbohydrate binding process is still important task and can be helpful for further lectin engineering by targeted mutagenesis methods. Lectins with tuned affinity can offer interesting perspectives in biomedical or biotechnology. Ourwork is focused on the engineering of previously well studied lectins PA-IIL [1], CV-IIL [2], RS-IIL [3] and BC2L-A [4] from the PA-IIL lectin family. Effects of the mutations on the individual lectin binding behaviour were studied by isothermal titration microcalorimetry method (ITC).
Název v anglickém jazyce
Studies of mutant lectin binding behaviour by microcalorimetry
Popis výsledku anglicky
Bacterial lectins help pathogens in adhesion to sugar moieties presented on the host cell surface. Therefore, lectins from pathogenic bacteria and their adhesion modes are the subject of intense study. On the other hand, understanding of the basic principles of the lectin-carbohydrate binding process is still important task and can be helpful for further lectin engineering by targeted mutagenesis methods. Lectins with tuned affinity can offer interesting perspectives in biomedical or biotechnology. Ourwork is focused on the engineering of previously well studied lectins PA-IIL [1], CV-IIL [2], RS-IIL [3] and BC2L-A [4] from the PA-IIL lectin family. Effects of the mutations on the individual lectin binding behaviour were studied by isothermal titration microcalorimetry method (ITC).
Klasifikace
Druh
O - Ostatní výsledky
CEP obor
CE - Biochemie
OECD FORD obor
—
Návaznosti výsledku
Projekt
—
Návaznosti
S - Specificky vyzkum na vysokych skolach
Ostatní
Rok uplatnění
2014
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů