Structure of the ordered hydration of amino acids in proteins: analysis of crystal structures

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F15%3A00457403" target="_blank" >RIV/86652036:_____/15:00457403 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1107/S1399004715015679" target="_blank" >http://dx.doi.org/10.1107/S1399004715015679</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1107/S1399004715015679" target="_blank" >10.1107/S1399004715015679</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Structure of the ordered hydration of amino acids in proteins: analysis of crystal structures

Popis výsledku v původním jazyce

Crystallography provides unique information about the arrangement of water molecules near protein surfaces. Using a nonredundant set of 2818 protein crystal structures with a resolution of better than 1.8 angstrom, the extent and structure of the hydration shell of all 20 standard amino-acid residues were analyzed as function of the residue conformation, secondary structure and solvent accessibility. The results show how hydration depends on the amino-acid conformation and the environment in which it occurs. After conformational clustering of individual residues, the density distribution of water molecules was compiled and the preferred hydration sites were determined as maxima in the pseudo-electron-density representation of water distributions. Manyhydration sites interact with both main-chain and side-chain amino-acid atoms, and several occurrences of hydration sites with less canonical contacts, such as carbon-donor hydrogen bonds, OH-pi interactions and off-plane interactions wit

Název v anglickém jazyce

Structure of the ordered hydration of amino acids in proteins: analysis of crystal structures

Popis výsledku anglicky

Crystallography provides unique information about the arrangement of water molecules near protein surfaces. Using a nonredundant set of 2818 protein crystal structures with a resolution of better than 1.8 angstrom, the extent and structure of the hydration shell of all 20 standard amino-acid residues were analyzed as function of the residue conformation, secondary structure and solvent accessibility. The results show how hydration depends on the amino-acid conformation and the environment in which it occurs. After conformational clustering of individual residues, the density distribution of water molecules was compiled and the preferred hydration sites were determined as maxima in the pseudo-electron-density representation of water distributions. Manyhydration sites interact with both main-chain and side-chain amino-acid atoms, and several occurrences of hydration sites with less canonical contacts, such as carbon-donor hydrogen bonds, OH-pi interactions and off-plane interactions wit

Druh

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

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

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Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

Acta Crystallographica Section D-Biological Crystalloghraphy

ISSN

1399-0047

e-ISSN

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Svazek periodika

71

Číslo periodika v rámci svazku

11

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

25

Strana od-do

2178-2202

Kód UT WoS článku

000364553500003

EID výsledku v databázi Scopus

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