All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

Visual Analysis of Protein–Protein Interaction Docking Models Using COZOID Tool

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14330%2F20%3A00115070" target="_blank" >RIV/00216224:14330/20:00115070 - isvavai.cz</a>

  • Result on the web

    <a href="https://link.springer.com/protocol/10.1007%2F978-1-4939-9873-9_7" target="_blank" >https://link.springer.com/protocol/10.1007%2F978-1-4939-9873-9_7</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1007/978-1-4939-9873-9_7" target="_blank" >10.1007/978-1-4939-9873-9_7</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Visual Analysis of Protein–Protein Interaction Docking Models Using COZOID Tool

  • Original language description

    Networks of protein–protein interactions (PPI) constitute either stable or transient complexes in every cell. Most of the cellular complexes keep their function, and therefore stay similar, during evolution. The evolutionary constraints preserve most cellular functions via preservation of protein structures and interactions. The evolutionary conservation information is utilized in template-based approaches, like protein structure modeling or docking. Here we use the combination of the template-free docking method with conservation-based selection of the best docking model using our newly developed COZOID tool. We describe a step-by-step protocol for visual selection of docking models, based on their similarity to the original protein complex structure. Using the COZOID tool, we first analyze contact zones of the original complex structure and select contact amino acids for docking restraints. Then we model and dock the homologous proteins. Finally, we utilize different analytical modes of our COZOID tool to select the docking models most similar to the original complex structure.

  • Czech name

  • Czech description

Classification

  • Type

    C - Chapter in a specialist book

  • CEP classification

  • OECD FORD branch

    10201 - Computer sciences, information science, bioinformathics (hardware development to be 2.2, social aspect to be 5.8)

Result continuities

  • Project

    <a href="/en/project/LQ1601" target="_blank" >LQ1601: CEITEC 2020</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2020

  • Confidentiality

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

Data specific for result type

  • Book/collection name

    Protein-Protein Interaction Networks

  • ISBN

    9781493998722

  • Number of pages of the result

    14

  • Pages from-to

    81-94

  • Number of pages of the book

    291

  • Publisher name

    Humana Press Inc

  • Place of publication

    New York, NY

  • UT code for WoS chapter

    000558678200008