dc.contributor.authorJose, Asial Ignacio
dc.date.accessioned2014-04-11T05:27:58Z
dc.date.accessioned2017-07-23T08:42:47Z
dc.date.available2014-04-11T05:27:58Z
dc.date.available2017-07-23T08:42:47Z
dc.date.copyright2014en_US
dc.date.issued2014
dc.identifier.citationJose, A. I. (2014). Novel methods and screens for portein stability engineering. Doctoral thesis, Nanyang Technological University, Singapore.
dc.identifier.urihttp://hdl.handle.net/10356/58910
dc.description.abstractProtein stability is often a limiting factor in the development of commercial proteins and biopharmaceuticals, as well as for biochemical and structural studies. In this thesis, I present different methods developed with the aim of improving protein stability, either by mutagenesis or by interaction with a protein partner.For protein stabilization through mutagenesis, a new high-throughput colony-based stability screen is described, which is a direct and biophysical read-out of intrinsic protein stability. As the method is generic and activity independent, it can easily be applied to a wide range of proteins. For protein stabilization through interaction with a protein partner, the use of phage display was explored. As an alternative and complement to phage display, I present the development of a new biophysical screen that monitors protein stabilization upon binding in cells and crude extracts, and its use in de novo binder generation using an autonomous VH domain as scaffold.en_US
dc.format.extent169 p.en_US
dc.language.isoenen_US
dc.subjectDRNTU::Science::Biological sciences::Biophysicsen_US
dc.subjectDRNTU::Science::Biological sciences::Biochemistryen_US
dc.subjectDRNTU::Science::Biological sciences::Molecular biologyen_US
dc.titleNovel methods and screens for portein stability engineeringen_US
dc.typeThesis
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.contributor.supervisorNordlund Paer Lennart
dc.contributor.supervisorTobias Cornviken_US
dc.description.degreeDOCTOR OF PHILOSOPHY (SBS)en_US


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