Action of Carboxypeptidase Toward Peptides Containing Unnatural Aromatic Amino Acids
β Scribed by Dunn, F. W.; Dittmer, K.
- Book ID
- 121143049
- Publisher
- American Association for the Advancement of Science
- Year
- 1950
- Tongue
- English
- Weight
- 237 KB
- Volume
- 111
- Category
- Article
- ISSN
- 0036-8075
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It is now routine using automatic Edman microsequencing to determine the primary structure of peptides or proteins containing natural amino acids; however, a deficiency in the ability to readily sequence peptides containing unnatural amino acids remains. With the advent of synthetic peptide chemistr
The interactions with DNA of tetrapeptide amides containing lysine a t the N-terminal position and aromatic amino acids a t the second and fourth positions (Ala a t position three), 1-6, have been investigated by nmr, CD, and viscometric methods. Tetrapeptides with N-terminal lysine and a single aro
A series of oligopeptides containing aromatic and basic residues were synthesized and their interactions with double-stranded nucleic acids studied by proton and phosphorus NMR, viscometry, and DNA melting temperature (T m ). The oligopeptides prepared contain two aromatic amino acids (phenylalanine