Polymorphism and conformational dynamics of F1-ATPases from bacterial membranes. A model for the regulation of these enzymes on the basis of molecular plasticity. [electronic resource]
Producer: 19820917Description: 233-65 p. digitalISSN:- 0006-3002
- ATP Synthetase Complexes
- Adenosine Diphosphate -- metabolism
- Adenosine Triphosphatases -- antagonists & inhibitors
- Adenosine Triphosphate -- metabolism
- Bacteria -- enzymology
- Cations, Divalent
- Cell Membrane -- enzymology
- Chloroplasts -- enzymology
- Drug Stability
- Enterococcus faecalis -- enzymology
- Escherichia coli -- enzymology
- Immunologic Techniques
- Liposomes -- metabolism
- Macromolecular Substances
- Magnesium -- pharmacology
- Micrococcus -- enzymology
- Mitochondria -- enzymology
- Molecular Weight
- Multienzyme Complexes -- metabolism
- Phosphotransferases -- metabolism
- Protein Binding
- Protein Conformation
- Proton-Translocating ATPases
- Solubility
- Structure-Activity Relationship
- Trypsin
- Zinc -- pharmacology
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Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Review
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