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Nuclear magnetic resonance study of side-chain conformation of tyrosyl residue in [Met5]-enkephalin. Solvent and temperature dependence

✍ Scribed by J. Kobayashi; T. Higashijima; U. Nagai; T. Miyazawa


Book ID
113126384
Publisher
Elsevier Science
Year
1980
Weight
831 KB
Volume
621
Category
Article
ISSN
0005-2795

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Solid-State nuclear magnetic resonance i
✍ Paul A. Burke; Robert G. Griffin; Alexander M. Klibanov πŸ“‚ Article πŸ“… 1993 πŸ› John Wiley and Sons 🌐 English βš– 808 KB

Tyrosyl ring motions in a-lytic protease were investigated by solid-state deuterium nuclear magnetic resonance (NMR) spectroscopy in lyophilized enzyme powder, in powder suspended in organic solvents, and in aqueous crystals. Ring flipping rates were determined by examining deuterium quadrupole echo