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- W2085454635 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." @default.
- W2085454635 created "2016-06-24" @default.
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- W2085454635 date "2010-11-01" @default.
- W2085454635 modified "2023-09-27" @default.
- W2085454635 title "Far-Infrared Spectroscopy of Protein Higher-Order Structures" @default.
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- W2085454635 doi "https://doi.org/10.1366/000370210793335025" @default.
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