Role of conformational flexibility for enzymatic activity in NADH oxidase from Thermus thermophilus. [electronic resource]
Producer: 20040211Description: 4887-97 p. digitalISSN:- 0014-2956
- Binding Sites
- Catalysis
- Circular Dichroism
- Crystallography, X-Ray
- Dimerization
- Flavins -- chemistry
- Kinetics
- Models, Molecular
- Multienzyme Complexes -- chemistry
- NADH, NADPH Oxidoreductases -- chemistry
- Protein Conformation
- Spectrometry, Fluorescence
- Temperature
- Thermodynamics
- Thermus thermophilus -- enzymology
- Time Factors
- Tryptophan -- chemistry
- Urea -- pharmacology
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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