Large, dynamic, multi-protein complexes: a challenge for structural biology

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F14%3A00436076" target="_blank" >RIV/61388963:_____/14:00436076 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1088/0953-8984/26/46/463103" target="_blank" >http://dx.doi.org/10.1088/0953-8984/26/46/463103</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1088/0953-8984/26/46/463103" target="_blank" >10.1088/0953-8984/26/46/463103</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Large, dynamic, multi-protein complexes: a challenge for structural biology

Popis výsledku v původním jazyce

Structural biology elucidates atomic structures of macromolecules such as proteins, DNA, RNA, and their complexes to understand the basic mechanisms of their functions. Among proteins that pose the most difficult problems to current efforts are those which have several large domains connected by long, flexible polypeptide segments. Although abundant and critically important in biological cells, such proteins have proven intractable by conventional techniques. This gap has recently led to the advancementof hybrid methods that use state-of-the-art computational tools to combine complementary data from various high-and low-resolution experiments. In this review, we briefly discuss the individual experimental techniques to illustrate their strengths and limitations, and then focus on the use of hybrid methods in structural biology. We describe how representative structures of dynamic multi-protein complexes are obtained utilizing the EROS hybrid method that we have co-developed.

Název v anglickém jazyce

Large, dynamic, multi-protein complexes: a challenge for structural biology

Popis výsledku anglicky

Structural biology elucidates atomic structures of macromolecules such as proteins, DNA, RNA, and their complexes to understand the basic mechanisms of their functions. Among proteins that pose the most difficult problems to current efforts are those which have several large domains connected by long, flexible polypeptide segments. Although abundant and critically important in biological cells, such proteins have proven intractable by conventional techniques. This gap has recently led to the advancementof hybrid methods that use state-of-the-art computational tools to combine complementary data from various high-and low-resolution experiments. In this review, we briefly discuss the individual experimental techniques to illustrate their strengths and limitations, and then focus on the use of hybrid methods in structural biology. We describe how representative structures of dynamic multi-protein complexes are obtained utilizing the EROS hybrid method that we have co-developed.

Druh

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

CEP obor

CF - Fyzikální chemie a teoretická chemie

OECD FORD obor

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Projekt

<a href="/cs/project/LO1302" target="_blank" >LO1302: InterBioMed</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2014

Kód důvěrnosti údajů

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

Název periodika

Journal of Physics-Condensed Matter

ISSN

0953-8984

e-ISSN

—

Svazek periodika

26

Číslo periodika v rámci svazku

46

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

11

Strana od-do

"463103/1"-"463103/11"

Kód UT WoS článku

000343796400004

EID výsledku v databázi Scopus

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