Analysis of the internal motion of free and ligand‐bound human lysozyme by use of15N NMR relaxation measurement: A comparison with those of hen lysozyme
Author:
Affiliation:
1. Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka 812‐8582, Japan
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1110/ps.9.9.1669
Reference42 articles.
1. Effects of ion binding on the backbone dynamics of calbindin D9k determined by nitrogen-15 NMR relaxation
2. Refinement of human lysozyme at 1.5 Å resolution analysis of non-bonded and hydrogen-bond interactions
3. Crystallographic studies of the activity of hen egg-white lysozyme
4. Defining the Orientation of the 15N Shielding Tensor Using 15N NMR Relaxation Data for a Protein in Solution
5. Structural Determinants of Protein Dynamics: Analysis of 15N NMR Relaxation Measurements for Main-Chain and Side-Chain Nuclei of Hen Egg White Lysozyme
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