Enzyme-inhibitor complexes of lysozyme with glucosamine inhibitors A molecular dynamics study through 2H-NMR

László Szilágyi, P. Forgó

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

2H relaxation measurements coupled with multiple specific 2H labeling have provided insight into the molecular dynamics of N-acetyl-d-glucosamine (GlcNAc) inhibitors bound to lysozyme. Deuteron T1 and T2 data for the bound state of methyl α- and -β-GlcNAc 2H-labeled in the glycosidic methyl and C2 positions have been derived from measurements at different enzyme/inhibitor ratios. Rotational correlation times calculated therefrom for the labeled sites indicate, in both cases, tight binding for the sugar ring (τb = 3.0 × 10-9 s) accompanied by fast internal rotation, about one axis, of the glycosidic methyl groups (τr = 5.5-7.6 × 10-11 s). The small but consistent difference in the rates of internal rotation for the α- and β-anomeric inhibitors may be indicative of different solution structures of the enzyme-inhibitor complexes.

Original languageEnglish
Pages (from-to)89-96
Number of pages8
JournalBiophysical Chemistry
Volume40
Issue number1
DOIs
Publication statusPublished - 1991

Fingerprint

enzyme inhibitors
Glucosamine
lysozyme
Enzyme Inhibitors
Molecular Dynamics Simulation
Muramidase
inhibitors
Molecular dynamics
Nuclear magnetic resonance
molecular dynamics
nuclear magnetic resonance
Deuterium
sugars
Sugars
Labeling
marking
deuterons
rings

Keywords

  • Enzyme-inhibitor complex
  • Lysozyme
  • Molecular dynamics
  • N-Acetyl-d-glucosamine
  • NMR, H-

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Physical and Theoretical Chemistry

Cite this

Enzyme-inhibitor complexes of lysozyme with glucosamine inhibitors A molecular dynamics study through 2H-NMR. / Szilágyi, László; Forgó, P.

In: Biophysical Chemistry, Vol. 40, No. 1, 1991, p. 89-96.

Research output: Contribution to journalArticle

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