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AuthorLazoutine, Alexei A.dc.contributor.author
Date of accession2016-03-14T13:39:09Zdc.date.accessioned
Available in OPARU since2016-03-14T13:39:09Zdc.date.available
Year of creation2004dc.date.created
AbstractNowadays functional polymers tend to solve more and more complex problems, e.g. controlled drug release, various external fields sensitivity. Biopolymers (proteins, DNA, RNA) take special place among them in complexity of solved problems. It caused substantially by their unique sequence of monomeric units where the sequences of majority of synthetic polymers have a Marcovian statistics. The range of use of polymers could be expanded farther via sequence formation in synthetic copolymers. A technique for synthesis of copolymers called conformation-dependent sequence design was suggested some time ago. The base of the technique is the following: units are modified on the base of their position in specifically chosen conformation. Copolymers with sequence designed in such way have different macroscopic characteristics in comparison with random copolymers. The present work is aimed at further development of the influence of three different modifications of the model on conformational properties of polymer. That influence is investigated. 1. Other rules of using the 'parent' globular conformation for the preparation of the primary sequence. The scheme of primary sequence design uses the principle of flat layer separation in the center of the globule conformation. The system of this copolymer shows the restorations of elements of microstructure. 2. Introduction of other interaction types in addition to the routinely used volume interaction can influence the properties of the synthesized polymers. Several models of saturating bond, which has some properties of hydrogen bond, were used. 3. Accounting for the details of monomer structure in the model. The aggregation behavior of copolymers in the frame of a model considering amphiphilic nature of monomeric units usually considered hydrophilic was studied in this work. This model confirms a qualitative difference between the copolymers with different statistics.dc.description.abstract
Languageendc.language.iso
PublisherUniversität Ulmdc.publisher
LicenseStandard (Fassung vom 03.05.2003)dc.rights
Link to license texthttps://oparu.uni-ulm.de/xmlui/license_v1dc.rights.uri
KeywordConformational behaviour of polymersdc.subject
KeywordHP-copolymerdc.subject
KeywordProtein-like copolymersdc.subject
LCSHCopolymers. Conformation. Computer simulationdc.subject.lcsh
TitleInfluence of link structure, interaction potential and the primary sequence on the conformation properties of protein-like copolymers: computer simulationdc.title
Resource typeDissertationdc.type
DOIhttp://dx.doi.org/10.18725/OPARU-419dc.identifier.doi
URNhttp://nbn-resolving.de/urn:nbn:de:bsz:289-vts-52579dc.identifier.urn
GNDCopolymeredc.subject.gnd
FacultyFakultät für Naturwissenschaftenuulm.affiliationGeneral
Date of activation2005-05-03T11:33:03Zuulm.freischaltungVTS
Peer reviewneinuulm.peerReview
Shelfmark print versionZ: J-H 10.758 ; W: W-H 8.713uulm.shelfmark
DCMI TypeTextuulm.typeDCMI
VTS-ID5257uulm.vtsID
CategoryPublikationenuulm.category
University Bibliographyjauulm.unibibliographie


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