Item type:Thesis, Open Access

β-Turns jenseits natürlicher Limitierungen - Flexible und rigide Dipeptidbausteine in der Proteinumgebung des Foldon-Trimers und seinem isolierten b-hairpin

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Date

2015-11-30

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Philipps-Universität Marburg
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Abstract

β-turns mediate diverse protein recognition processes in the human organism, although dihedral angle preferences of canonical amino acids limit accessible β-turn geometries and their mobility. Organic chemistry can go beyond these limitations: Synthetic b-turn dipeptide building blocks with more flexible or rigid backbones outpace the characteristics of canonical amino acids. That leads to significantly altered populations of the natural stand-alone hairpin (Ala12–Ser24) derived from the Foldon miniprotein due to their differing turn inducing capacities. The influence of the same β-turn mimetics on the b-hairpin was also studied within the complex protein environment of the trimeric Foldon by analyzing several NMR based parameters and their melting tempera-tures. In contrast to the isolated b-hairpin, for which rigid β-turn mimetics in the i+1 and i+2-turn positions lead to highly populated folds, the best combinations to fulfill the structural and dy-namical requirements of the Foldon protein-protein interfaces between the monomer chains are natural b-amino acids. The obtained data raises questions on whether highly stabilized, designed b-hairpins are suitable as b-sheet model systems to simulate evolutionarily optimized proteins in a complete fashion, especially in their dynamic behavior.

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Dates
Created: 2015Issued: 2015-11-30
DOI
https://doi.org/10.17192/z2015.0471
Faculty
Fachbereich Chemie
Publisher
Philipps-Universität Marburg
Language
ger
Data types
DoctoralThesis
Keywords
Faltungspopulation, BindungsepitopPeptidsyntheseprotein designfold populationProteindesignpeptide synthesisβ-hairpin peptidesbinding epitopeβ-hairpin Peptide
DFG-subjects
PeptideMagnetische KernresonanzChemische Synthese
DDC-Numbers
540
License
https://rightsstatements.org/vocab/InC-NC/1.0/
URI
https://open.uni-marburg.de/handle/10.17192/z2015.0471
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Körling, Matthias: β-Turns jenseits natürlicher Limitierungen - Flexible und rigide Dipeptidbausteine in der Proteinumgebung des Foldon-Trimers und seinem isolierten b-hairpin. : Philipps-Universität Marburg 2015-11-30. DOI: https://doi.org/10.17192/z2015.0471.

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This item has been published with the following license: In Copyright