Low-Frequency Spectroscopic Analysis of Monomeric and Fibrillar Lysozyme-Reference-Cited by-同舟云学术

Low-Frequency Spectroscopic Analysis of Monomeric and Fibrillar Lysozyme

Published:2011-03 Issue:3 Volume:65 Page:260-264
ISSN:0003-7028
Container-title:Applied Spectroscopy
language:en
Short-container-title:Appl Spectrosc

Author:

Zakaria Hidayatul A.¹,Fischer Bernd M.¹,Bradley Andrew P.¹,Jones Inke¹,Abbott Derek¹,Middelberg Anton P. J.¹,Falconer Robert J.¹

Affiliation:

1. Australian Institute for Bioengineering and Nanotechnology, The University of Queensland, Brisbane QLD 4072, Australia (H.A.Z., A.P.J.M., R.J.F.); French-German Research Institute of Saint-Louis (ISL), 5 rue du General de Cassagnou, 68301 Saint-Louis Cedex, France (B.M.F.); School of Information Technology and Electrical Engineering, The University of Queensland, Brisbane QLD 4072, Australia (A.P.B.); and Department of Electrical and Electronic Engineering, The University of Adelaide, South Australia, SA...

Abstract

Terahertz time-domain spectroscopy (THz-TDS) and Fourier transform infrared (FT-IR) spectroscopy were used to generate far-infrared and low-frequency spectral measurements of monomeric lysozyme and lysozyme fibrils. The formation of lysozyme fibrils was verified by the Thioflavin T assay and transmission electron microscopy (TEM). It was evident in the FT-IR spectra that between 150 and 350 cm−1 the two spectra diverge, with the lysozyme fibrils showing higher absorbance intensity than the monomeric form. The broad absorption phenomenon is likely due to light scattered from the fibrillar architecture of lysozyme fibrils as supported by simulation of Rayleigh light scattering. The lack of discrete phonon-like peaks suggest that far-infrared spectroscopy cannot detect vibrational modes between the highly ordered hydrogen-bonded beta-pleated sheets of the lysozyme subunit.

Publisher

SAGE Publications

Subject

Spectroscopy,Instrumentation

Link

http://journals.sagepub.com/doi/pdf/10.1366/10-06162

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