Interaction of aromatic residues of proteins with nucleic acids. Circular dichroism studies of the binding of oligopeptides to poly(adenylic acid)
✍ Scribed by Durand, Maurice; Maurizot, Jean C.; Borazan, Hanna N.; Helene, Claude
- Book ID
- 126120100
- Publisher
- American Chemical Society
- Year
- 1975
- Tongue
- English
- Weight
- 825 KB
- Volume
- 14
- Category
- Article
- ISSN
- 0006-2960
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## Abstract The circular dichroic properties of H‐Gly‐Phe‐(Gly)~__n__~‐Trp‐Gly‐OH (II, __n__ = 0,1,2) and of related simpler peptides, such as H‐Phe‐Gly‐OH, H‐Gly‐Phe‐OH, H‐Gly‐Phe‐Gly‐OH, H‐Phe‐Trp‐OH, H‐Phe‐Trp‐Gly‐OH, and H‐Gly‐Phe‐Trp‐OH in water and trifluoroethanol solutions are investigated.
## Abstract | I. | Introduction | 306 | | II. | Supramolecular Structure Characterization | 308 | | | A. A Protein Is Used as a “Hook” | 309 | | | 1. Immuno‐Precipitation | 309 | | | 2. Tagging with a Poly‐Histidine Sequence | 310 | | | 3. Direct Analysis of Large Protein Complexes | 3