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

Kód výsledku v 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>

Nalezeny alternativní kódy

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

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

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

Popis výsledku anglicky

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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

BO - Biofyzika

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2012

Kód důvěrnosti údajů

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

Název periodika

Journal of Molecular Recognition

ISSN

0952-3499

e-ISSN

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Svazek periodika

25

Číslo periodika v rámci svazku

11

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

12

Strana od-do

604-615

Kód UT WoS článku

000310555100011

EID výsledku v databázi Scopus

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