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Towards a better understanding of the specificity of protein-protein interaction

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F12%3A10133499" target="_blank" >RIV/00216208:11310/12:10133499 - isvavai.cz</a>

  • Alternative codes found

    RIV/86652036:_____/12:00385763 RIV/61388963:_____/12:00385763

  • Result on the web

    <a href="http://dx.doi.org/10.1002/jmr.2219" target="_blank" >http://dx.doi.org/10.1002/jmr.2219</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1002/jmr.2219" target="_blank" >10.1002/jmr.2219</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Towards a better understanding of the specificity of protein-protein interaction

  • Original language description

    In order to predict interaction interface for proteins, it is crucial to identify their characteristic features controlling the interaction process. We present analysis of 69 crystal structures of dimer protein complexes that provides a basis for reasonable description of the phenomenon. Interaction interfaces of two proteins at amino acids level were localized and described in terms of their chemical composition, binding preferences, and residue interaction energies utilizing Amber empirical force field. The characteristic properties of the interaction interface were compared against set of corresponding intramolecular binding parameters for amino acids in proteins. It has been found that geometrically distinct clusters of large hydrophobic amino acids (leucine, valine, isoleucine, and phenylalanine) as well as polar tyrosines and charged arginines are signatures of the proteinprotein interaction interface. At some extent, we can generalize that proteinprotein interaction (seen throug

  • Czech name

  • Czech description

Classification

  • Type

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

  • CEP classification

    BO - Biophysics

  • 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>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2012

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Journal of Molecular Recognition

  • ISSN

    0952-3499

  • e-ISSN

  • Volume of the periodical

    25

  • Issue of the periodical within the volume

    11

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    12

  • Pages from-to

    604-615

  • UT code for WoS article

    000310555100011

  • EID of the result in the Scopus database