Dynamic features of cAMP-dependent protein kinase revealed by apoenzyme crystal structure. [electronic resource]
Producer: 20030417Description: 159-71 p. digitalISSN:- 0022-2836
- Adenosine -- metabolism
- Adenosine Triphosphate -- metabolism
- Amino Acid Sequence
- Animals
- Apoenzymes -- chemistry
- Binding Sites
- Crystallography, X-Ray
- Cyclic AMP-Dependent Protein Kinases -- chemistry
- Hydrophobic and Hydrophilic Interactions
- Mice
- Models, Molecular
- Molecular Sequence Data
- Protein Conformation
- Protein Subunits
- Ribose -- metabolism
- Static Electricity
- Substrate Specificity
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Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
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