Please use this identifier to cite or link to this item:
Full metadata record
DC FieldValueLanguage
dc.contributor.authorPhillips, Margareten
dc.identifier.citationPhillips, M. (2016). The use of nuclear magnetic resonance in study of structurally dynamic membrane proteins. Doctoral thesis, Nanyang Technological University, Singapore.en
dc.description.abstractNuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool used to study both the structure and dynamics of proteins. NMR can be used for studying both crystal-like and intrinsically disordered proteins. However, for a large class of partially structured or flexible and dynamic proteins, the methodological problems such as in-homogeneous resonance line broadening which results in partial or complete loss of signal to background noise, may appear insurmountable. These partially structured proteins form a large portion of the eukaryotic proteome and play crucial roles in many important cellular processes. For my Ph.D. thesis, with the help of several NMR methods and cost-effective sample preparation, we explored the structure and dynamics of such proteins belonging to the essential class of adaptor coil-coiled proteins and membrane proteins. These proteins are either part of a dynamic complex or themselves form tetrameric channels. In particular our focus was on the following proteins: human Stromal Interaction Molecule 1 (hSTIM1), human Presenilin Enhancer-2 (hPEN-2) and E.coli water channel Aquaporin Z (AqpZ).en
dc.format.extent201 p.en
dc.subjectDRNTU::Science::Biological sciencesen
dc.titleThe use of nuclear magnetic resonance in study of structurally dynamic membrane proteinsen
dc.contributor.schoolSchool of Biological Sciencesen
dc.description.degreeDOCTOR OF PHILOSOPHY (SBS)en
item.fulltextWith Fulltext-
Appears in Collections:SBS Theses
Files in This Item:
File Description SizeFormat 
Thesis_MargaretPhillips.pdf5.89 MBAdobe PDFThumbnail

Google ScholarTM




Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.