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Statements

Subject Item
n2:RIV%2F00216224%3A14310%2F07%3A00020642%21RIV09-GA0-14310___
rdf:type
skos:Concept n19:Vysledek
dcterms:description
Lectins are proteins of nonimmune origin that non-enzymatically selectively bind to mono or oligosaccharides. Multifarious activity of carbohydrates in biophysiological pathway, such as immune activity, tumor metastasis, cell-cell recognition, bacterial pathogenecity, open an avenue for the lectin-carbohydrate interaction research, which is also a big challenge for theoretical modeling due to the polar flexible saccharide moiety. One of the lectins, PA-IIL that produced by Pseudomonas aeruginosa, which play significant role in cystic fibrosis disease, motivated our study on PA-IIL-carbohydrate interactions. The structure can provide a static view of the macromolecules, but for the full understanding of protein-ligand interactions it is necessary to know all the accessible spatial orientations of the ligand in the receptor binding pocket. It is often seen that the binding energy calculated over the sampled structure by molecular dynamics could give the insight of the interactions between protein and li Lectins are proteins of nonimmune origin that non-enzymatically selectively bind to mono or oligosaccharides. Multifarious activity of carbohydrates in biophysiological pathway, such as immune activity, tumor metastasis, cell-cell recognition, bacterial pathogenecity, open an avenue for the lectin-carbohydrate interaction research, which is also a big challenge for theoretical modeling due to the polar flexible saccharide moiety. One of the lectins, PA-IIL that produced by Pseudomonas aeruginosa, which play significant role in cystic fibrosis disease, motivated our study on PA-IIL-carbohydrate interactions. The structure can provide a static view of the macromolecules, but for the full understanding of protein-ligand interactions it is necessary to know all the accessible spatial orientations of the ligand in the receptor binding pocket. It is often seen that the binding energy calculated over the sampled structure by molecular dynamics could give the insight of the interactions between protein and li Lectins are proteins of nonimmune origin that non-enzymatically selectively bind to mono or oligosaccharides. Multifarious activity of carbohydrates in biophysiological pathway, such as immune activity, tumor metastasis, cell-cell recognition, bacterial pathogenecity, open an avenue for the lectin-carbohydrate interaction research, which is also a big challenge for theoretical modeling due to the polar flexible saccharide moiety. One of the lectins, PA-IIL that produced by Pseudomonas aeruginosa, which play significant role in cystic fibrosis disease, motivated our study on PA-IIL-carbohydrate interactions. The structure can provide a static view of the macromolecules, but for the full understanding of protein-ligand interactions it is necessary to know all the accessible spatial orientations of the ligand in the receptor binding pocket. It is often seen that the binding energy calculated over the sampled structure by molecular dynamics could give the insight of the interactions between protein and li
dcterms:title
Computational Studies on PA-IIL Lectin-Carbohydrate Interactions Computational Studies on PA-IIL Lectin-Carbohydrate Interactions Computational Studies on PA-IIL Lectin-Carbohydrate Interactions
skos:prefLabel
Computational Studies on PA-IIL Lectin-Carbohydrate Interactions Computational Studies on PA-IIL Lectin-Carbohydrate Interactions Computational Studies on PA-IIL Lectin-Carbohydrate Interactions
skos:notation
RIV/00216224:14310/07:00020642!RIV09-GA0-14310___
n3:aktivita
n20:P
n3:aktivity
P(GD204/03/H016)
n3:dodaniDat
n5:2009
n3:domaciTvurceVysledku
Mishra, Navnit Kumar n11:4347374 n11:5522064 n11:3466272
n3:druhVysledku
n16:D
n3:duvernostUdaju
n8:S
n3:entitaPredkladatele
n6:predkladatel
n3:idSjednocenehoVysledku
414622
n3:idVysledku
RIV/00216224:14310/07:00020642
n3:jazykVysledku
n15:eng
n3:klicovaSlova
Computational studies; Molecular modeling; Interaction energy calculation
n3:klicoveSlovo
n7:Computational%20studies n7:Interaction%20energy%20calculation n7:Molecular%20modeling
n3:kontrolniKodProRIV
[C908BC64952F]
n3:mistoKonaniAkce
Nove Hrady, Czech Republic
n3:mistoVydani
Nove Hrady, Czech Republic
n3:nazevZdroje
In Materials Structure in Chemistry, Biology, Physics and Technology. Praha : Česká a slovenská krystalografická společnost
n3:obor
n4:CE
n3:pocetDomacichTvurcuVysledku
4
n3:pocetTvurcuVysledku
5
n3:projekt
n13:GD204%2F03%2FH016
n3:rokUplatneniVysledku
n5:2007
n3:tvurceVysledku
Mishra, Navnit Kumar Koča, Jaroslav Kriz, Zdenek Wimmerová, Michaela Kulhánek, Petr
n3:typAkce
n17:CST
n3:zahajeniAkce
2007-03-30+02:00
s:issn
1211-5894
s:numberOfPages
1
n18:hasPublisher
Česká a slovenská krystalografická společnost
n14:organizacniJednotka
14310