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TRITON: graphic software for rational engineering of enzymes

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F01%3A00002737" target="_blank" >RIV/00216224:14310/01:00002737 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    TRITON: graphic software for rational engineering of enzymes

  • Original language description

    The engineering of enzymes for improving their catalytic properties is one of the present-day challenges of biochemistry and molecular biology. The rational engineering of a given enzyme requires an understanding of the structural features determining its catalytic efficiency. In particular, a protein engineer has to know which amino acid residues of the protein are involved in the catalysis and how to modify them to achieve an increased activity. The availability of the three-dimensional structure of the protein, preferably in the complex with the substrate, makes a significant step forward in the understanding the protein-ligand interactions. However, this is just an initial step in understanding how these interactions influence the conversion of thesubstrate to the product. The catalytic efficiency of enzymes is usually determined by their ability to stabilise the transition state of their reactions. Consequently, an examination of the enzyme-substrate complex, i.e. the educt struc

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • 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)

Others

  • Publication year

    2001

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Trends in Biochemical Sciences

  • ISSN

  • e-ISSN

  • Volume of the periodical

    28

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    3

  • Pages from-to

    71

  • UT code for WoS article

  • EID of the result in the Scopus database