Segmental Motion of Subsite C of Hen Egg-White Lysozyme

Fluorescence Depolarization Studies of Kyn62-Lysozyme as an Active Analogue

Shoji Yamashita, Etsuko Nishimoto, Nobuyuki Yamasaki

Research output: Contribution to journalComment/debate

3 Citations (Scopus)

Abstract

The dynamical properties of subsite C of hen egg-white lysozyme were investigated using Kyn62-lysozyme as an active analogue. Time-resolved fluorescence depolarization studies showed that the segmental motion of kynurenine which was important in subsite C was described with two components of which the rotational correlation times were ϕ1=150ps and ϕ2=1.4ns, respectively. Although these two segmental motions retained 90% of motional freedom, the slower motion was completely restricted and the degree of freedom was lost to 40% during the interaction with oligomers of N-acetyl-D-glucosamine.

Original languageEnglish
Pages (from-to)1579-1580
Number of pages2
JournalBioscience, Biotechnology and Biochemistry
Volume59
Issue number8
DOIs
Publication statusPublished - Jan 1 1995

Fingerprint

Egg White
Depolarization
Muramidase
Fluorescence
Kynurenine
Acetylglucosamine
Oligomers
hen egg lysozyme

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

Cite this

Segmental Motion of Subsite C of Hen Egg-White Lysozyme : Fluorescence Depolarization Studies of Kyn62-Lysozyme as an Active Analogue. / Yamashita, Shoji; Nishimoto, Etsuko; Yamasaki, Nobuyuki.

In: Bioscience, Biotechnology and Biochemistry, Vol. 59, No. 8, 01.01.1995, p. 1579-1580.

Research output: Contribution to journalComment/debate

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