The solution structure of the outer membrane lipoprotein OmlA from Xanthomonas axonopodis pv. citri reveals a protein fold implicated in protein-protein interaction. [electronic resource]
Producer: 20080806Description: 2051-64 p. digitalISSN:- 1097-0134
- Amino Acid Motifs
- Amino Acid Sequence
- Amino Acids, Aromatic -- chemistry
- Bacterial Outer Membrane Proteins -- chemistry
- Circular Dichroism
- Cysteine -- chemistry
- Deuterium Exchange Measurement
- Escherichia coli -- genetics
- Genes, Reporter
- Hydrophobic and Hydrophilic Interactions
- Lipoproteins -- chemistry
- Models, Molecular
- Molecular Sequence Data
- Molecular Weight
- Nuclear Magnetic Resonance, Biomolecular
- Promoter Regions, Genetic
- Protein Conformation
- Protein Folding
- Protein Sorting Signals
- Protein Structure, Secondary
- Protein Structure, Tertiary
- Proteins -- metabolism
- Recombinant Proteins -- chemistry
- Sequence Homology, Amino Acid
- Spectrophotometry, Ultraviolet
- Spectrum Analysis, Raman
- Xanthomonas axonopodis -- chemistry
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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