About: A systematic method for analysing the protein hydration structure of T4 lysozyme

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: A systematic method for analysing the protein hydration structure of T4 lysozyme Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
rdfs:seeAlso	http://dx.doi.org/10.1002/jmr.2290
Description	A systematic method for the analysis of the hydration structure of proteins is demonstrated on the case study of lysozyme. The method utilises multiple structural data of the same protein deposited in the protein data bank. Clusters of high water occupancy are localised and characterised in terms of their interaction with protein. It is shown that they constitute a network of interconnected hydrogen bonds anchored to the protein molecule. The high occupancy of the clusters does not directly correlate with water-protein interaction energy as was originally hypothesised. The highly occupied clusters rather correspond to the nodes of the hydration network that have the maximum number of hydrogen bonds including both the protein atoms and the surrounding water clusters. A systematic method for the analysis of the hydration structure of proteins is demonstrated on the case study of lysozyme. The method utilises multiple structural data of the same protein deposited in the protein data bank. Clusters of high water occupancy are localised and characterised in terms of their interaction with protein. It is shown that they constitute a network of interconnected hydrogen bonds anchored to the protein molecule. The high occupancy of the clusters does not directly correlate with water-protein interaction energy as was originally hypothesised. The highly occupied clusters rather correspond to the nodes of the hydration network that have the maximum number of hydrogen bonds including both the protein atoms and the surrounding water clusters. (en)
Title	A systematic method for analysing the protein hydration structure of T4 lysozyme A systematic method for analysing the protein hydration structure of T4 lysozyme (en)
skos:prefLabel	A systematic method for analysing the protein hydration structure of T4 lysozyme A systematic method for analysing the protein hydration structure of T4 lysozyme (en)
skos:notation	RIV/00216208:11310/13:10191799!RIV14-GA0-11310___
http://linked.open...avai/predkladatel	Přírodovědecká fakulta
http://linked.open...avai/riv/aktivita	I P
http://linked.open...avai/riv/aktivity	I, P(GAP208/10/0725), P(LH11020)
http://linked.open...iv/cisloPeriodika	10
http://linked.open...vai/riv/dodaniDat	2014
http://linked.open...aciTvurceVysledku	Kysilka, Jiří
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Univerzita Karlova v Praze / Přírodovědecká fakulta
http://linked.open...dnocenehoVysledku	59137
http://linked.open...ai/riv/idVysledku	RIV/00216208:11310/13:10191799
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	interaction enthalpy; cluster algorithm; X-ray crystallography; water; protein hydration structure (en)
http://linked.open.../riv/klicoveSlovo	cluster algorithm interaction enthalpy protein hydration structure X-ray crystallography water
http://linked.open...odStatuVydavatele	GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV	[B339E2C12154]
http://linked.open...i/riv/nazevZdroje	Journal of Molecular Recognition
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	1 (xsd:int)
http://linked.open...cetTvurcuVysledku	2 (xsd:int)
http://linked.open...vavai/riv/projekt	Systematic mapping of the conformational space of short peptides through molecular dynamics simulation - a way to understanding of protein structure formation. Studium mezimolekulových interakcí v molekulových krystalech a proteinech
http://linked.open...UplatneniVysledku	2013
http://linked.open...v/svazekPeriodika	26
http://linked.open...iv/tvurceVysledku	Kysilka, Jiří Vondrášek, Jiří
http://linked.open...ain/vavai/riv/wos	000323674900006
issn	0952-3499
number of pages	9 (xsd:int)
http://bibframe.org/vocab/doi	10.1002/jmr.2290
http://localhost/t...ganizacniJednotka	11310

Faceted Search & Find service v1.16.118 as of Jun 21 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 24 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software