Münster (Westfalen), Univ., Diss., 2004. / Computerdatei im Fernzugriff.

Freiburg (Breisgau), Universiẗat, Diss., 2001.

Halle, Wittenberg, University, Diss., 2001.

Freiburg (Breisgau), Universiẗat, Diss., 2002.

Bielefeld, University, Diss., 2003.

No description available.

This research includes two topics. The first topic is prepared a series of poly(methyl methacrylate) (PMMA)-based copolymers through free radical copolymerizations of methyl methacrylate in the presence of the either 2 - vinyl - 4,6 -diamino - 1, 3, 5triazine(VDAT) or vinylbenzyl -thymine (VBT). Using 1H nuclear magnetic resonance (NMR) spectroscopy, Fourier transform infrared (FTIR) spectroscopy, differential scanning calorimetry (DSC), we investigated the thermal properties and hydrogen-bonding interactions within blends of the two copolymers poly(2-vinyl-4,6-diamino-1,3,5-triazine-co-methyl methacrylate) (PVD AT-co-PMMA) and poly(vinylbenzylthymine-co-methyl methacrylate) (PVBT-co-PMMA). A large positive deviation in the behavior of the glass transition temperature determined by using the Kwei equation and DSC analyses indicated that strong multiple hydrogen-bonding interactions existed between the two copolymers. The FTIR and solid-state NMR spectroscopic analyses provided positive evidence for the presence of three hydrogen bonds between the diamino-1,3,5-triazine groups of PVDAT and thymine groups of PVBT. The second topic is synthesized a series of alkyne end-terminated poly(£^-Benzyl L-glutamate) (alkyne-PBLG), which was prepared by the ring-opening polymerization of the N-carboxyanhydride monomer of £^-Benzyl L-glutamate-carboxyanhydride. Then combination of the alkyne-PBLG with polyhedral oligomeric silsesquioxanes (POSS) with eight function groups are prepared through the click reation and formed a peptide-based block polymer with £\-helice and £]-sheet conformations. The thermal properties and structure of these polypeptides were characterized by using 1H NMR and FTIR. The FTIR, solid-state NMR and WXRD spectroscopic analyses provided evidence for the change of secondary structure between POSS and terminated peptide group, so that the conformation of £]-sheets and £\-helices would be influenced by the incorporation of POSS nanoparticle.

No description available.

Essen, Univ., Diss., 2000. / Computerdatei im Fernzugriff.

Duisburg, Universiẗat, Diss., 1997.