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Studying the Oligomerization of the Kinase Domain of Ephrin type-B Receptor 2 Using Analytical Ultracentrifugation and Development of a Program for Analysis of Acquired Data
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, The Institute of Technology.
2014 (English)Independent thesis Advanced level (degree of Master (Two Years)), 20 credits / 30 HE creditsStudent thesis
Abstract [en]

Ephrin type-B receptor 2 (EphB2) is a receptor tyrosine kinase which phosphorylates proteins and thereby regulates cell migration, vascular development, axon guidance synaptic plasticity, and formation of borders between tissues. It has been seen overexpressed in several cancers, which make it an interesting protein to study. In this thesis EphB2 kinase domain (KD) and juxtamembrane segment with kinase domain (JMS-KD) have been expressed, purified and studied using analytical ultracentrifugation to evaluate the oligomerisation of the KD and how the double mutation S677/680A affects this. A program for data analysis have been written and used for analysis of the acquired data. The values of the dissociation constant were 2.94±1.04 mM for KD wild type and 3.46±2.26 mM for JMS-KD wild type have been calculated. Due to varied problems with the measurements no data was acquired on the double mutant, and not enough data was gained to draw any conclusions. Additional experiments will be needed to understand the oligomerisation of this intriguing protein.

Place, publisher, year, edition, pages
2014. , 45 p.
Keyword [en]
Ephrin type-B receptor 2, EphB2, Analytical Ultracentrifugation, Oligomerization, Kinase Domain, Protein Expression, Protein Purification, Programming, Analysis of Data
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:liu:diva-110376ISRN: LITH-IFM-A-EX--14/2934--SEOAI: diva2:745161
Subject / course
Chemical Biology
Available from: 2015-06-01 Created: 2014-09-09 Last updated: 2015-06-01Bibliographically approved

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Master Thesis(1807 kB)31 downloads
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Lundberg, Alexander
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