Structures composing protein domains

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F13%3A10191621" target="_blank" >RIV/00216208:11310/13:10191621 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388971:_____/13:00399148 RIV/75010330:_____/13:00010097

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.biochi.2013.04.001" target="_blank" >http://dx.doi.org/10.1016/j.biochi.2013.04.001</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.biochi.2013.04.001" target="_blank" >10.1016/j.biochi.2013.04.001</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Structures composing protein domains

Popis výsledku v původním jazyce

This review summarizes available data concerning intradomain structures (IS) such as functionally important amino acid residues, short linear motifs, conserved or disordered regions, peptide repeats, broadly occurring secondary structures or folds, etc.IS form structural features (units or elements) necessary for interactions with proteins or non-peptidic ligands, enzyme reactions and some structural properties of proteins. These features have often been related to a single structural level (e.g. primary structure) mostly requiring certain structural context of other levels (e.g. secondary structures or supersecondary folds) as follows also from some examples reported or demonstrated here. In addition, we deal with some functionally important dynamicproperties of IS (e.g. flexibility and different forms of accessibility), and more special dynamic changes of IS during enzyme reactions and allosteric regulation. Selected notes concern also some experimental methods, still more necessar

Název v anglickém jazyce

Structures composing protein domains

Popis výsledku anglicky

This review summarizes available data concerning intradomain structures (IS) such as functionally important amino acid residues, short linear motifs, conserved or disordered regions, peptide repeats, broadly occurring secondary structures or folds, etc.IS form structural features (units or elements) necessary for interactions with proteins or non-peptidic ligands, enzyme reactions and some structural properties of proteins. These features have often been related to a single structural level (e.g. primary structure) mostly requiring certain structural context of other levels (e.g. secondary structures or supersecondary folds) as follows also from some examples reported or demonstrated here. In addition, we deal with some functionally important dynamicproperties of IS (e.g. flexibility and different forms of accessibility), and more special dynamic changes of IS during enzyme reactions and allosteric regulation. Selected notes concern also some experimental methods, still more necessar

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2013

Kód důvěrnosti údajů

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

Název periodika

Biochimie

ISSN

0300-9084

e-ISSN

—

Svazek periodika

95

Číslo periodika v rámci svazku

8

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

14

Strana od-do

1511-1524

Kód UT WoS článku

000321801500001

EID výsledku v databázi Scopus

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