Please use this identifier to cite or link to this item:
|Title:||The use of nuclear magnetic resonance in study of structurally dynamic membrane proteins||Authors:||Phillips, Margaret||Keywords:||DRNTU::Science::Biological sciences||Issue Date:||2016||Source:||Phillips, M. (2016). The use of nuclear magnetic resonance in study of structurally dynamic membrane proteins. Doctoral thesis, Nanyang Technological University, Singapore.||Abstract:||Nuclear 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).||URI:||https://hdl.handle.net/10356/68476||DOI:||10.32657/10356/68476||Fulltext Permission:||open||Fulltext Availability:||With Fulltext|
|Appears in Collections:||SBS Theses|
Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.