About: Is It Possible to Study Conformation of an Unpurified Protein?

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

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	Je možné studovat konformace %22nečistých%22 proteinů? (cs) During the last period enormous progress in protein conformation studies has been made thanks to the methods of X-ray crystalography as well as of NMR spectroscopy. These two methods are able to provide information about localization of individual atoms in three-dimensional structure of the protein. In addition to these %22absolute%22 methods, different quicker, cheaper and technically less demanding methods (circular dichroism, fluorimetry etc.) are available; they usually give sensitive information about changes in protein conformation and facilitate to compare structures of functionally analogical proteins.Chemical modifications of proteins have already been successfully performed in order to obtain information about localization of certain amino acid residues in protein globule [1,2]. These methods work on a simple principle: 1) To a native protein of known covalent structure a specific agent, which modifies a single (or limited number) amino acid side chain, is added. 2) The excess of the During the last period enormous progress in protein conformation studies has been made thanks to the methods of X-ray crystalography as well as of NMR spectroscopy. These two methods are able to provide information about localization of individual atoms in three-dimensional structure of the protein. In addition to these %22absolute%22 methods, different quicker, cheaper and technically less demanding methods (circular dichroism, fluorimetry etc.) are available; they usually give sensitive information about changes in protein conformation and facilitate to compare structures of functionally analogical proteins.Chemical modifications of proteins have already been successfully performed in order to obtain information about localization of certain amino acid residues in protein globule [1,2]. These methods work on a simple principle: 1) To a native protein of known covalent structure a specific agent, which modifies a single (or limited number) amino acid side chain, is added. 2) The excess of the (en)
Title	Is It Possible to Study Conformation of an Unpurified Protein? Is It Possible to Study Conformation of an Unpurified Protein? (en) Je možné studovat konformace %22nečistých%22 proteinů? (cs)
skos:prefLabel	Is It Possible to Study Conformation of an Unpurified Protein? Is It Possible to Study Conformation of an Unpurified Protein? (en) Je možné studovat konformace %22nečistých%22 proteinů? (cs)
skos:notation	RIV/60461373:22330/04:00012822!RIV/2005/GA0/223305/N
http://linked.open.../vavai/riv/strany	32
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(GA203/02/0922), Z(MSM 223300006)
http://linked.open...vai/riv/dodaniDat	2005
http://linked.open...aciTvurceVysledku	Šantrůček, Jiří Hynek, Radovan Kodíček, Milan Strohalm, Martin
http://linked.open.../riv/druhVysledku	D - Článek ve sborníku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Vysoká škola chemicko-technologická v Praze / Fakulta potravinářské a biochemické technologie
http://linked.open...dnocenehoVysledku	569022
http://linked.open...ai/riv/idVysledku	RIV/60461373:22330/04:00012822
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	tryptophan;tyrosine;surface accessibility;MALDI-TOF MS (en)
http://linked.open.../riv/klicoveSlovo	surface accessibility tryptophan tyrosine MALDI-TOF MS
http://linked.open...ontrolniKodProRIV	[272B00757BF9]
http://linked.open...v/mistoKonaniAkce	Olomouc, Czech Republic
http://linked.open...i/riv/mistoVydani	Olomouc
http://linked.open...i/riv/nazevZdroje	Acta Universitatis Palackianae Olomucensis, Facultas Rerum Naturalium, Chemica
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	4 (xsd:int)
http://linked.open...cetTvurcuVysledku	4 (xsd:int)
http://linked.open...vavai/riv/projekt	Application of MALDI-TOF (matrix assisted laser desorption ionisation - Time of Flight) mass spectrometry on the determination of protein conformation
http://linked.open...UplatneniVysledku	2004
http://linked.open...iv/tvurceVysledku	Hynek, Radovan Kodíček, Milan Šantrůček, Jiří Strohalm, Martin
http://linked.open...vavai/riv/typAkce	WRD - Světová
http://linked.open.../riv/zahajeniAkce	2004-08-31 (xsd:date)
http://linked.open...n/vavai/riv/zamer	http://linked.opendata.cz/resource/domain/vavai/zamer/MSM%20223300006
number of pages	1 (xsd:int)
http://purl.org/ne...btex#hasPublisher	Univerzita Palackého v Olomouci
https://schema.org/isbn	80-244-0882-1
http://localhost/t...ganizacniJednotka	22330

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