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|2010 ||Falconer, Robert J., Zakaria, Hidayatul A., Fan, Yuan Y., Bradley, Andrew P. and Middelberg, Anton P.J. (2010) Far-infrared spectroscopy of protein higher-order structures. Applied Spectroscopy, 64 11: 1259-1264.|
Far-infrared (FIR) spectroscopy in the spectral region of 50-450 cm -1 was used to study a series of protein higher-order structures constructed using ²-lactoglobulin and Polyomavirus capsid protein VP1. There were marked differences in the spectra for ²-lactoglobulin monomer and dimer and between untreated ß-lactoglobulin and heat-induced gels formed at neutral pH. Untreated ß-lactoglobulin and heat-induced gels formed at acidic pH exhibited little difference in their spectra. Assembly of the quaternary structure of Polyomavirus virus-like particles also caused large changes in the FIR spectra. These findings suggest that FIR spectroscopy may prove useful in studying some protein quaternary and higher-order structures. There was evidence of detection of ²-lactoglobulin dimerization, intermolecular disulfide bonding in heat-induced neutral gels, and Polyomavirus virus-like particle assembly but no evidence that FIR could detect ²-lactoglobulin fibrils with their polymeric structure and hydrogen-bonded intermolecular ²-pleated sheeting. © 2010 Society for Applied Spectroscopy.
|Ms Yuanyuan Fan, Prof. Andrew P. Bradley, Professor Anton Middelberg|
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|Links: ||Journal website|
|Keywords: ||Terahertz, Beta-lactoglobulin, Vibrational spectrometry, Amyloid, Fibril, Polyomavirus, Virus-like particle, Quaternary structure|