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
—