Probing the role of aromatic residues at the secondary saccharide-binding sites of human salivary alpha-amylase in substrate hydrolysis and bacterial binding. [electronic resource]
Producer: 20090107Description: 1232-48 p. digitalISSN:- 1089-8638
- Acarbose -- chemistry
- Amino Acids -- metabolism
- Bacterial Adhesion
- Bacterial Outer Membrane Proteins -- isolation & purification
- Binding Sites
- Carbohydrates -- chemistry
- Circular Dichroism
- Durapatite -- metabolism
- Humans
- Hydrolysis
- Kinetics
- Mutant Proteins -- metabolism
- Oligosaccharides -- chemistry
- Protein Structure, Secondary
- Salivary alpha-Amylases -- chemistry
- Starch -- metabolism
- Static Electricity
- Streptococcus gordonii -- metabolism
- Structure-Activity Relationship
- Substrate Specificity
- Surface Plasmon Resonance
- X-Ray Diffraction
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Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
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