NMR studies of the conformations and location of nucleotides bound to the Escherichia coli MutT enzyme. [electronic resource]
Producer: 19950601Description: 5577-86 p. digitalISSN:- 0006-2960
- Adenosine Triphosphate -- analogs & derivatives
- Amino Acid Sequence
- Bacterial Proteins -- chemistry
- Binding Sites
- Escherichia coli -- enzymology
- Escherichia coli Proteins
- Guanosine Triphosphate -- analogs & derivatives
- Magnetic Resonance Spectroscopy -- methods
- Models, Molecular
- Models, Structural
- Molecular Conformation
- Molecular Sequence Data
- Phosphoric Monoester Hydrolases -- chemistry
- Protein Conformation
- Protein Structure, Secondary
- Pyrophosphatases
- Sequence Homology, Amino Acid
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Publication Type: Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S.
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