Non-enzymatic extracellular proteins and their role in growth, defense, and metabolism
| dc.contributor.author | McDougall, Matthew Daniel | |
| dc.contributor.examiningcommittee | Tomy, Gregg (Chemistry) McKenna, Sean (Chemistry) Mishra, Suresh (Physiology and Pathophysiology) Heerklotz, Heiko (Bioss and Institute of Pharmaceutical Sciences, University of Freiburg) | en_US |
| dc.contributor.supervisor | Stetefeld, Joerg (Chemistry) | en_US |
| dc.date.accessioned | 2018-01-11T22:25:44Z | |
| dc.date.available | 2018-01-11T22:25:44Z | |
| dc.date.issued | 2016-11-30 | en_US |
| dc.date.issued | 2017-07-13 | en_US |
| dc.date.issued | 2017-10-11 | en_US |
| dc.degree.discipline | Chemistry | en_US |
| dc.degree.level | Doctor of Philosophy (Ph.D.) | en_US |
| dc.description.abstract | While enzymes can be easily categorized by their catalytic function, the functions of non-enzymatic proteins can be much more subtle. In the absence of experimental data, protein functions are often assigned based on sequence or domain conservation, but this can be misleading. Beginning with the human guidance protein Netrin-4, to the pit viper venom constituent Rhodocetin and its interaction integrin α2β1, a blood clotting protein, and finishing with Right Handed Coiled-Coil, a surface layer component of microorganisms that live in the harshest environments, this thesis brings to light new knowledge on three extracellular systems where structural characterization and subsequent validation were used to clarify their functions or their mechanism of action. | en_US |
| dc.description.note | February 2018 | en_US |
| dc.identifier.citation | Reuten, R., Patel, T.R., McDougall, M. et al. Structural decoding of netrin-4 reveals a regulatory function towards mature basement membranes. Nat. Commun. 7, 13515 (2016) | en_US |
| dc.identifier.citation | Eble, J. A., McDougall, M. et al. Dramatic and concerted conformational changes enable rhodocetin to block α2β1 integrin selectively. PLoS Biol. 15, e2001492 (2017) | en_US |
| dc.identifier.citation | McDougall, M. et al. Archaea S-layer nanotube from a “black smoker” in complex with cyclo-octasulfur (S8) rings. Proteins. 85, 2209–2216 (2017) | en_US |
| dc.identifier.uri | http://hdl.handle.net/1993/32809 | |
| dc.language.iso | eng | en_US |
| dc.publisher | Nature Communications | en_US |
| dc.publisher | PLOS Biology | en_US |
| dc.publisher | Proteins: Structure, Function, and Bioinformatics | en_US |
| dc.rights | open access | en_US |
| dc.subject | Structural Biology | en_US |
| dc.subject | Xray Diffraction | en_US |
| dc.subject | Netrin | en_US |
| dc.subject | Nanotube | en_US |
| dc.subject | Hemostasis | en_US |
| dc.subject | Archaea | en_US |
| dc.subject | Sulfur Respiration | en_US |
| dc.title | Non-enzymatic extracellular proteins and their role in growth, defense, and metabolism | en_US |
| dc.type | doctoral thesis | en_US |