Structural analysis of threonine 342 mutants of soybean beta-amylase: role of a conformational change of the inner loop in the catalytic mechanism. [electronic resource]
Producer: 20050525Description: 5106-16 p. digitalISSN:- 0006-2960
- Amino Acid Sequence
- Amino Acid Substitution
- Catalytic Domain
- Crystallography, X-Ray
- Hydrogen Bonding
- Kinetics
- Ligands
- Maltose -- chemistry
- Models, Molecular
- Multiprotein Complexes
- Mutagenesis, Site-Directed
- Mutation
- Protein Conformation
- Recombinant Proteins -- chemistry
- Sequence Homology, Amino Acid
- Glycine max -- enzymology
- Static Electricity
- Threonine -- chemistry
- beta-Amylase -- chemistry
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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