Segmental motion of subsite C of hen egg-white lysozyme: fluorescence depolarization studies of Kyn62-lysozyme as an active analogue.
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 phi 1 = 150 ps and phi 2 = 1.4 ns, 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.
Yamashita
S
S
Institute of Biophysics, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.
Nishimoto
E
E
Yamasaki
N
N
D000818:Animals; D002244:Carbon; D002645:Chickens; D004527:Egg Proteins / Q000737:chemistry; D005454:Fluorescence Polarization; D009113:Muramidase / Q000737:chemistry*; D013329:Structure-Activity Relationship
D004527:Egg Proteins; D002244:Carbon; C022664:kynurenine 62-lysozyme; D009113:Muramidase