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Main Title: Structural examination of hydrophobic tunnels in proteins
Translated Title: Strukturelle Untersuchung von hydrophoben Tunneln in Proteinen
Author(s): Kalms, Jacqueline
Advisor(s): Scheerer, Patrick
Referee(s): Scheerer, Patrick
Hildebrandt, Peter
Granting Institution: Technische Universität Berlin
Type: Doctoral Thesis
Language Code: en
Abstract: Enzymes are the biological macromolecular catalysts of life, which work with high substrate specificity, under fine-tuned conditions compared to chemical catalysts. The majority of the catalytic centres of enzymes are located deeply within the protein matrix. To provide efficient substrate accessibility to the active site most proteins offer permanent or transient tunnels as transport pathways. In this thesis, the substrate tunnels of the O2-tolerant membrane-bound [NiFe] hydrogenase (MBH) from the β-proteobacterium Ralstonia eutropha (Re) and the lipoxygenase (LOX) from the human pathogen Pseudomonas aeruginosa (Pa) are studied with protein X-ray crystallography, novel gas-pumping techniques for protein crystal derivatisation, molecular dynamics (MD) simulations, computational tunnel calculations, site-directed mutagenesis as well as basic structure ligand modelling.
Enzyme sind makromolekulare Biokatalysatoren und im Vergleich zu chemischen Katalysatoren arbeiten sie mit hoher Substratspezifizität, unter spezifisch angepassten Bedingungen. Die meisten katalytischen Zentren in Enzymen sind tief in der Proteinmatrix verborgen. Damit die Substrate das aktive Zentrum erreichen können, bilden ein Großteil dieser Proteine permanente oder transiente Tunnel als Transportwege aus. In dieser Dissertation werden für Substrate zugängliche Tunnel der sogenannten sauerstoff-toleranten, membrangebundenen [NiFe] hydrogenase (MBH) von dem β-Proteobakterium Ralstonia eutropha (Re) und der Lipoxygenase (LOX) von dem humanen Pathogen Pseudomonas aeruginosa (Pa) mit Hilfe der Röntgenkristallographie, Molekulardynamik-Simulationen (MD), computergestützten Tunnel-Berechnungen, molekular-biologischen Untersuchungen (Punktmutationen) und Proteinliganden-Modellierungen untersucht.
Exam Date: 10-May-2017
Issue Date: 2018
Date Available: 11-Apr-2018
DDC Class: 572 Biochemie
Subject(s): oxygen-tolerant [NiFe] hydrogenase
iron-sulfur cluster
X-ray crystallography
crystal derivatisation
sauerstofftolerante [NiFe] hydrogenase
Eisen-Schwefel Cluster
Kristall Derivatisierung
Appears in Collections:Inst. Chemie » Publications

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