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|Title:||Terahertz spectroscopic differentiation of microstructures in protein gels|
|Citation:||Clinical Research in Cardiology, 2009; 17(15):13102-13115|
|Publisher:||Dr Dietrich Steinkopff Verlag|
|Gretel M. Png, Robert J. Falconer, Bernd M. Fischer, Hidayatul A. Zakaria, Samuel P. Mickan, Anton P. J. Middelberg and Derek Abbott|
|Abstract:||We demonstrate that terahertz (THz) spectroscopy can be used to differentiate soft protein microstructures. Differentiation of soft microstructures in gels has to date been performed using optical imaging techniques (e.g. electron microscope), but a non-destructive differentiation tool is lacking. Particulate and fine-stranded (fibrillar) soft protein microstructures are of interest, particularly to medical researchers, because they form from naturally occurring proteins that are thought to be involved in several human diseases, such as Alzheimer's disease. In this study, globular beta-lactoglobulin structures with diameters of 2 microm, and fibrillar structures with diameters less than 0.03 microm are observed between 0.8 and 1.5 THz. Results show that the globular structures have a decline in THz transmission when compared to the fibrillar ones. The cause of this decline is possibly due to Rayleigh scattering from the globular microstructures.|
|Keywords:||Animals; Cattle; Humans; Alzheimer Disease; Proteins; Lactoglobulins; Gels; Spectrophotometry, Infrared; Spectroscopy, Fourier Transform Infrared; Molecular Conformation; Protein Conformation; Terahertz Spectroscopy; Optics and Photonics; Hydrogen-Ion Concentration; Spectrophotometry|
|Description:||© 2009 Optical Society of America|
|Appears in Collections:||Electrical and Electronic Engineering publications|
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