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Self-Folding of Single Chain Polymers: Towards Synthetic Biomacromolecule Design

Altintas, Özcan

Abstract:

The emulation of natural processes and the design of chemical reaction sequences inspired by nature is one of the most important driving forces for synthetic macromolecular design. Many proteins fold in solution to yield delicate molecular assemblies stabilized by non-covalent. The key binding principle in nature revolves around the formation of hydrogen bonds. It seems appropriate to transfer this concept when attempting to fold synthetic macromolecules to mimic naturally occurring systems.
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Volltext §
DOI: 10.5445/IR/1000028913
Cover der Publikation
Zugehörige Institution(en) am KIT Institut für Technische Chemie und Polymerchemie (ITCP)
Publikationstyp Hochschulschrift
Publikationsjahr 2012
Sprache Englisch
Identifikator urn:nbn:de:swb:90-289135
KITopen-ID: 1000028913
Verlag Karlsruher Institut für Technologie (KIT)
Art der Arbeit Dissertation
Fakultät Fakultät für Chemie und Biowissenschaften (CHEM-BIO)
Institut Institut für Technische Chemie und Polymerchemie (ITCP)
Prüfungsdaten 20.07.2012
Schlagwörter self-folding, single chain, synthetic protein, ATRP, Click chemisrty
Referent/Betreuer Barner-Kowollik, C.
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