Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/68476
Full metadata record
DC FieldValueLanguage
dc.contributor.authorPhillips, Margareten
dc.date.accessioned2016-05-26T04:18:46Zen
dc.date.available2016-05-26T04:18:46Zen
dc.date.issued2016en
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.identifier.urihttps://hdl.handle.net/10356/68476en
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.language.isoenen
dc.subjectDRNTU::Science::Biological sciencesen
dc.titleThe use of nuclear magnetic resonance in study of structurally dynamic membrane proteinsen
dc.typeThesisen
dc.contributor.schoolSchool of Biological Sciencesen
dc.description.degreeDOCTOR OF PHILOSOPHY (SBS)en
dc.identifier.doi10.32657/10356/68476en
item.grantfulltextopen-
item.fulltextWith Fulltext-
Appears in Collections:SBS Theses
Files in This Item:
File Description SizeFormat 
Thesis_MargaretPhillips.pdf5.89 MBAdobe PDFThumbnail
View/Open

Google ScholarTM

Check

Altmetric


Plumx

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