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Protein engineering of lectins - in silico and in vitro approaches

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F11%3A00050180" target="_blank" >RIV/00216224:14740/11:00050180 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Protein engineering of lectins - in silico and in vitro approaches

  • Original language description

    rotein-carbohydrate interactions are usually characterized by a low affinity for monovalent ligands that is balanced by multivalency resulting in high avidity for ligands with several potential epitops. However, recent characterization of lectins involved in pathogenesis has demonstrated their much higher affinity even towards monosaccharide than that observed for plant or animal lectins [1]. This feature allows to use such lectins as a more/less specific tool, for example, for evaluation of protein glycosylation or isolation of glyco-conjugates. Random mutagenesis is often used in protein engineering for producing proteins with altered or improved properties. In our work several methodical directions have been applied. Error-prone PCR is based on error-prone DNA polymerase which introduces nucleotide changes during extension of amplified DNA.

  • Czech name

  • Czech description

Classification

  • Type

    O - Miscellaneous

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2011

  • Confidentiality

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