Summary
The conformations of thermolysin synthetic substrates in H2O/D2O (9/1) and glycerol-d 5 (5 M) are investigated using two-dimensional nuclear magnetic resonance spectroscopy and molecular modeling. The structures obtained from molecular modeling and NMR studies are compared. Comparisons of these structures with bound inhibitor in the active site of thermolysin are also discussed.
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Baltora-Rosset, S., Marty, D., Dupradeau, FY. et al. Micro-environment effect on the structure of synthetic substrates of thermolysin. Lett Pept Sci 4, 391–395 (1997). https://doi.org/10.1007/BF02442905
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DOI: https://doi.org/10.1007/BF02442905