Structural and molecular mechanism for autoprocessing of MARTX toxin of Vibrio cholerae at multiple sites. [electronic resource]
Producer: 20091106Description: 26557-68 p. digitalISSN:- 1083-351X
- Alanine -- chemistry
- Amino Acid Sequence
- Arginine -- chemistry
- Binding Sites -- genetics
- Catalytic Domain
- Cholera Toxin -- chemistry
- Crystallization
- Electrophoresis, Polyacrylamide Gel
- Hydrophobic and Hydrophilic Interactions
- Leucine -- chemistry
- Lysine -- chemistry
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Phytic Acid -- chemistry
- Protein Binding
- Protein Folding
- Protein Structure, Tertiary
- Static Electricity
- Thermodynamics
- Trypsin -- metabolism
- Vibrio cholerae -- genetics
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Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.
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