Birch pollen profilin: structural organization and interaction with poly-(L-proline) peptides as revealed by NMR. [electronic resource]
Producer: 19970923Description: 291-5 p. digitalISSN:- 0014-5793
- Acanthamoeba -- chemistry
- Amino Acid Sequence
- Animals
- Binding Sites
- Cell Adhesion Molecules -- metabolism
- Cloning, Molecular
- Contractile Proteins
- Cytoskeletal Proteins
- Escherichia coli
- Magnetic Resonance Spectroscopy
- Microfilament Proteins -- chemistry
- Molecular Sequence Data
- Peptides -- metabolism
- Phosphoproteins -- metabolism
- Plant Proteins -- chemistry
- Pollen -- chemistry
- Profilins
- Protein Binding
- Protein Structure, Secondary
- Proteins -- metabolism
- Recombinant Proteins -- chemistry
- Trees
- Vasodilator-Stimulated Phosphoprotein
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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