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.
All Science Journal Classification (ASJC) codes
- Analytical Chemistry
- Applied Microbiology and Biotechnology
- Molecular Biology
- Organic Chemistry