"0"^^ . . . . "2008-06-02+02:00"^^ . . "Spectroscopic analysis of the hinge peptide conformation and flexibility resulted in a consistent and reasonably complete picture. The peptide stays in a left handed helical conformation of the Polyproline II type and rather drastic intervention have to"@en . "1"^^ . . "Neuvedeno."@en . "1"^^ . "GA203/02/0328" . . . "Chiroptical properties, conformation and dynamical behaviour of the middle sized oligopeptide having structural domains with different flexibility"@en . "Vibrational circular dichroism (VCD) spectroscopy is potentially capable to provide rather detailed information about three dimensional structure and dynamics of the difficult-to-investigate class of middle sized molecules, e.g. oligopeptides. We intend to investigate this possibility in depth using several classes of oligopeptides in the molecules of which there are either distinct domains differring in flexibility and conformation or where rigid domains are connected with flexible links. Such molecules provide a good possibility to apply ab initio techniques to interpretation of vibrational optical activity data via the technique of transferring molecular property tensors. We have selected as the main goal the so-called hinge peptide (fragment of human igG1) in which two rigid octapeptide chains rich in proline are connected via flexible disulfide links. As model systems we will also investigate dioxopiperazine molecules containing basic amino acid residues embedded in a peptide"@en . "Vibra\u010Dn\u00ED cirkul\u00E1rn\u00ED dichroismus (VCD) je s nejv\u011Bt\u0161\u00ED pravd\u011Bpodobnost\u00ED schopen poskytovat detailn\u00ED informace o trojrozm\u011Brn\u00E9 struktu\u0159e a dynamick\u00E9m chov\u00E1n\u00ED st\u0159edn\u011B velk\u00FDch molekul (nap\u0159. oligopeptid\u016F), kter\u00E9 je zpravidla obt\u00ED\u017En\u00E9 jin\u00FDmi technikami studovat. M\u00E1me v \u00FAmyslu prozkoumat tuto mo\u017Enost u\u017Eit\u00EDm n\u011Bkolika typ\u016F oligopeptid\u016F, jejich\u017E spole\u010Dn\u00FDm rysem je bu\u010F p\u0159\u00EDtomnost odd\u011Blen\u00FDch oblast\u00ED, kter\u00E9 se li\u0161\u00ED konformac\u00ED nebo dynamikou, p\u0159\u00EDpadn\u011B takov\u00FDch molekul, v nich\u017E oblasti s rigidn\u00EDm uspo\u0159\u00E1d\u00E1n\u00EDm jsou propojeny flexibiln\u00ED spojkou. Takov\u00E9 molekuly poskytuj\u00ED mo\u017Enost aplikace ab initio technik k interpretaci dat vibra\u010Dn\u00ED optick\u00E9 aktivity technikou p\u0159enosu tenzor\u016F molekul\u00E1rn\u00EDch vlastnost\u00ED. Jako hlavn\u00ED c\u00EDl jsme zvolili tak zvan\u00FD %22hinge pepti%22 (fragment lidsk\u00E9ho imunoglobulinu igGl), v jeho\u017E molekule jsou dva rigidn\u00ED \u0159et\u011Bzce oktapeptidu (bohat\u00E9 na prolin) propojeny pohybliv\u00FDmi disulfidick\u00FDmi m\u016Fstky. Jako modelov\u00E9 syst\u00E9my budeme rovn\u011B\u017E zkoumat molekuly dioxopiperazin\u016F obsahuj\u00EDc\u00ED bazick\u00E9 aminokyseliny," . "Spektroskopick\u00E1 anal\u00FDza konformace a flexibility hinge peptidu poskytla konsistentn\u00ED a ucelen\u00FD obraz.\u00A0 Peptid si zachov\u00E1v\u00E1 konformaci typu levoto\u010Div\u00E9 \u0161roubovice polyprolin II a k jej\u00EDmu p\u0159echodu na jin\u00FD konforma\u010Dn\u00ED typ jsou pot\u0159ebn\u00E9 pom\u011Brn\u011B drastick\u00E9 z\u00E1s"@cs . . . "Chiroptick\u00E9 vlastnosti, konformace a dynamick\u00E9 chov\u00E1n\u00ED st\u0159edn\u011B velk\u00E9ho oligopeptidu se strukturn\u00EDmi dom\u00E9nami o v\u00FDrazn\u011B odli\u0161n\u00E9 flexibilit\u011B" . . . . . . "14"^^ . . "14"^^ . . . "http://www.isvav.cz/projectDetail.do?rowId=GA203/02/0328"^^ . . . . .