Pub No:
28
Title:
The Role of Distortion in the Lysozyme Mechanism .
Authors:
Sykes, B.D., Patt, S.L., and David Dolphin
Journal:
Cold Spring Harbor Symp. Quantitative Biology, XXXVI,
Year:
1971
Pages:
29-33
Abstract:
Using fourier transform NMR spectroscopy, the lysozyme mechanism was studied by investigation of the glucose ring of GNAc-β-(1 → 4)-G-β-(1)-C6H4NO2-p (I) and the reducing muramic acid ring of GNAc-β-(1 → 4)-MurNAc-β-(1 → 4)-GlcNAc-β-(1 → 4)-MurNAc (II). It was found that, bound to lysozyme, the glucose group of I is not distorted, or else a very small fraction is distorted. On the other hand, II bound to lysozyme is distorted.

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