Assessing the Functional Structure of Molecular Transporters by EPR Spectroscopy
Seiten
2014
|
2012
Springer Berlin (Verlag)
978-3-642-43795-3 (ISBN)
Springer Berlin (Verlag)
978-3-642-43795-3 (ISBN)
This book uses an innovative approach to assess the local structure and dynamics of biological and synthetic amphiphilic macromolecules capable of transporting small molecules, using electron paramagnetic resonance (EPR) spectroscopy.
In his thesis, Matthias Junk takes an innovative approach to assess the local structure and dynamics of biological and synthetic amphiphilic macromolecules capable of transporting small molecules. Replacing the latter with stable radicals, he uses state-of-the-art electron paramagnetic resonance (EPR) spectroscopy to describe the highly relevant transport function from the viewpoint of the guest molecules. Such, he demonstrates that the functional structure of human serum albumin in solution significantly differs from its crystal structure - a consequence of the protein's adaptability to host various endogenous compounds and drug molecules. Further, he shows that the thermal collapse of thermoresponsive hydrogels and dendronized polymers leads to static and dynamic heterogeneities on the nanoscale. These heterogeneities bear consequences for the material's hosting properties and enable unforeseen complex catalytic functionalities.
In his thesis, Matthias Junk takes an innovative approach to assess the local structure and dynamics of biological and synthetic amphiphilic macromolecules capable of transporting small molecules. Replacing the latter with stable radicals, he uses state-of-the-art electron paramagnetic resonance (EPR) spectroscopy to describe the highly relevant transport function from the viewpoint of the guest molecules. Such, he demonstrates that the functional structure of human serum albumin in solution significantly differs from its crystal structure - a consequence of the protein's adaptability to host various endogenous compounds and drug molecules. Further, he shows that the thermal collapse of thermoresponsive hydrogels and dendronized polymers leads to static and dynamic heterogeneities on the nanoscale. These heterogeneities bear consequences for the material's hosting properties and enable unforeseen complex catalytic functionalities.
Electron Paramagnetic Resonance Theory.- The Functional Structure of Human Serum Albumin.- Copper Complexes of Star-Shaped Cholic Acid Oligomers with 1,2,3-Triazole Moieties.- Nano-Inhomogeneities in Structure and Reactivity of Thermoresponsive Hydrogels.- Thermoresponsive Spin-Labeled Hydrogels as Separable DNP Polarizing Agents.- Local Nanoscopic Heterogeneities in Thermoresponsive Dendronized Polymers.
| Erscheint lt. Verlag | 22.2.2014 |
|---|---|
| Reihe/Serie | Springer Theses |
| Zusatzinfo | XVI, 212 p. |
| Verlagsort | Berlin |
| Sprache | englisch |
| Maße | 155 x 235 mm |
| Gewicht | 352 g |
| Themenwelt | Naturwissenschaften ► Chemie ► Organische Chemie |
| Technik ► Maschinenbau | |
| Schlagworte | binding sites of albumin, fatty acids, transport p • binding sites of albumin, fatty acids, transport protein • biomimetic systems • cholic acids • DNP • dynamics of macromolecular systems • EPR/ESR spectroscopy • LCST dynamic nuclear polarization • metal ion sensor • thermoresponsive polymer • umbrella shaped molecules |
| ISBN-10 | 3-642-43795-8 / 3642437958 |
| ISBN-13 | 978-3-642-43795-3 / 9783642437953 |
| Zustand | Neuware |
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