Temperature dependence of near-IR excited Raman spectra of crystalline hen egg-white lysozyme.
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.
Nara
M
M
Laboratory of Chemistry, College of Liberal Arts and Sciences, Tokyo Medical and Dental University, Ichikawa, Chiba 272-0827, Japan. nara.las@tmd.ac.jp
Sakamoto
A
A
Yamamichi
J
J
Tasumi
M
M
D000818:Animals; D002645:Chickens; D003460:Crystallization; D005260:Female; D009113:Muramidase / Q000737:chemistry*; D010063:Ovum / Q000201:enzymology; D013059:Spectrum Analysis, Raman; D013816:Thermodynamics
D009113:Muramidase