Temperature dependence of near-IR excited Raman spectra of crystalline hen egg-white lysozyme.
Biopolymers
; 62(3): 168-72, 2001.
Article
en En
| MEDLINE
| ID: mdl-11343287
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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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Muramidasa
Límite:
Animals
Idioma:
En
Revista:
Biopolymers
Año:
2001
Tipo del documento:
Article
País de afiliación:
Japón