Temperature dependence of near-IR excited Raman spectra of crystalline hen egg-white lysozyme

Biopolymers
M NaraM Tasumi

Abstract

Near-IR excited Raman spectroscopy was applied to examine the structural change of hen egg-white lysozyme in tetragonal crystals at low temperatures. There was little difference found in the amide I and amide III regions between the spectra observed at 77 and 298 K, suggesting that the secondary structures of lysozyme were conserved in the temperature range from 77 to 298 K. Several bands arising from the protein side chains, particularly the methylene and phenylalanyl groups, showed significant changes in either intensity or bandwidth (or in both of them) on going from 77 to 298 K. Some of the spectral changes occurred gradually over the wide temperature range, and others occurred abruptly at around 200-240 K. The implications of these findings are discussed.

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Citations

Nov 13, 2003·Journal of Colloid and Interface Science·Marco LattuadaMassimo Morbidelli
May 15, 2012·Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy·Vladislava VoiciukGediminas Niaura
Nov 4, 2008·Biosensors & Bioelectronics·Gobind DasEnzo Di Fabrizio
May 6, 2006·Analytical Biochemistry·Corasi OrtizDor Ben-Amotz
Oct 23, 2012·The Journal of Physical Chemistry. B·Francesco D'AmicoClaudio Masciovecchio
Apr 6, 2013·The Journal of Physical Chemistry. B·Vitaly KocherbitovGediminas Niaura

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