## Abstract The conformational state of the [3.3.3]propellane framework for 14โhydroxymodhephene was determined by extensive application of oneโ and twoโdimensional ^1^H and ^13^C NMR spectroscopy combined with xโray diffraction studies of a synthesized derivative, spectral simulation and molecular
X-Ray Diffraction and Molecular Model Building Studies of The Interaction of Actinomycin with Nucleic Acids
โ Scribed by HAMILTON, L. D.; FULLER, W.; REICH, E.
- Book ID
- 109627923
- Publisher
- Nature Publishing Group
- Year
- 1963
- Tongue
- English
- Weight
- 347 KB
- Volume
- 198
- Category
- Article
- ISSN
- 0028-0836
- DOI
- 10.1038/198538b0
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Proteinase K, the extracellular serine endopeptidase (E.C.3.4.21.14) from the fungus Tritirachium album limber, is homologous to the bacterial subtilisin proteases. The binding geometry of the synthetic inhibitor carbobenzoxy-Ala-Phechloromethyl ketone to the active site of proteinase K was first de