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Far-Infrared Spectroscopy of Protein Higher-Order Structures

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Abstract:

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 β-lactoglobulin and polyomavirus capsid protein VP1. There were marked differences in the spectra for β-lactoglobulin monomer and dimer and between untreated β-lactoglobulin and heat-induced gels formed at neutral pH. Untreated β-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 β-lactoglobulin dimerization, intermolecular disulfide bonding in heat-induced neutral gels, and polyomavirus virus-like particle assembly but no evidence that FIR could detect β-lactoglobulin fibrils with their polymeric structure and hydrogen-bonded intermolecular β-pleated sheeting.

Keywords: AMYLOID; BETA-LACTOGLOBULIN; FIBRIL; POLYOMAVIRUS; QUARTERNARY STRUCTURE; TERAHERTZ; VIBRATIONAL SPECTROMETRY; VIRUS-LIKE PARTICLE; β-LACTOGLOBULIN

Document Type: Research Article

DOI: http://dx.doi.org/10.1366/000370210793335025

Affiliations: 1: The University of Queensland, NCRIS Biotechnology Products, Australian Institute for Bioengineering and Nanotechnology, Brisbane QLD 4072, Australia. r.falconer@uq.edu.au 2: The University of Queensland, Centre for Biomolecular Engineering, Australian Institute for Bioengineering and Nanotechnology, Brisbane QLD 4072, Australia 3: The University of Queensland, School of Information Technology and Electrical Engineering, Brisbane QLD 4072, Australia

Publication date: November 1, 2010

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