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Statements

Subject Item
n2:RIV%2F60461373%3A22330%2F04%3A00012822%21RIV%2F2005%2FGA0%2F223305%2FN
rdf:type
n9:Vysledek skos:Concept
dcterms:description
Je možné studovat konformace %22nečistých%22 proteinů? 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
dcterms:title
Is It Possible to Study Conformation of an Unpurified Protein? Je možné studovat konformace %22nečistých%22 proteinů? Is It Possible to Study Conformation of an Unpurified Protein?
skos:prefLabel
Is It Possible to Study Conformation of an Unpurified Protein? Je možné studovat konformace %22nečistých%22 proteinů? Is It Possible to Study Conformation of an Unpurified Protein?
skos:notation
RIV/60461373:22330/04:00012822!RIV/2005/GA0/223305/N
n3:strany
32
n3:aktivita
n8:Z n8:P
n3:aktivity
P(GA203/02/0922), Z(MSM 223300006)
n3:dodaniDat
n11:2005
n3:domaciTvurceVysledku
n10:1120530 n10:9046976 n10:6936903 n10:2194538
n3:druhVysledku
n16:D
n3:duvernostUdaju
n7:S
n3:entitaPredkladatele
n22:predkladatel
n3:idSjednocenehoVysledku
569022
n3:idVysledku
RIV/60461373:22330/04:00012822
n3:jazykVysledku
n18:eng
n3:klicovaSlova
tryptophan;tyrosine;surface accessibility;MALDI-TOF MS
n3:klicoveSlovo
n5:MALDI-TOF%20MS n5:surface%20accessibility n5:tryptophan n5:tyrosine
n3:kontrolniKodProRIV
[272B00757BF9]
n3:mistoKonaniAkce
Olomouc, Czech Republic
n3:mistoVydani
Olomouc
n3:nazevZdroje
Acta Universitatis Palackianae Olomucensis, Facultas Rerum Naturalium, Chemica
n3:obor
n12:CE
n3:pocetDomacichTvurcuVysledku
4
n3:pocetTvurcuVysledku
4
n3:projekt
n14:GA203%2F02%2F0922
n3:rokUplatneniVysledku
n11:2004
n3:tvurceVysledku
Hynek, Radovan Šantrůček, Jiří Kodíček, Milan Strohalm, Martin
n3:typAkce
n21:WRD
n3:zahajeniAkce
2004-08-31+02:00
n3:zamer
n19:MSM%20223300006
s:numberOfPages
1
n6:hasPublisher
Univerzita Palackého v Olomouci
n17:isbn
80-244-0882-1
n15:organizacniJednotka
22330