Synthesis and Conformation of Sequential Polypeptides of L-Alanine and β-Aminobutyric Acid
| Autor: | Murray Goodman, S. St. Pierre, R. T. Ingwall |
|---|---|
| Rok vydání: | 1976 |
| Předmět: |
chemistry.chemical_classification
Alanine Circular dichroism Condensation polymer Spectrophotometry Infrared integumentary system Polymers and Plastics Protein Conformation Stereochemistry Aminobutyrates Circular Dichroism Organic Chemistry Infrared spectroscopy Polymer Random coil Inorganic Chemistry Hexafluoroacetone chemistry.chemical_compound Protein structure chemistry Materials Chemistry Spectrophotometry Ultraviolet Peptides |
| Zdroj: | Macromolecules. 9:1-6 |
| ISSN: | 1520-5835 0024-9297 |
| DOI: | 10.1021/ma60049a001 |
| Popis: | Sequential polypeptides with the repeating units L-alanyl-(S)-beta-aminobutyric acid, L-alanyl-(R)-beta-aminobutyric acid, and L-alanyl-(R,S)-beta-aminobutyric acid have been synthesized by polycondensation of the N-hydroxysuccinimide ester hydrochloride salts of the corresponding dipeptides. Circular dichroism and infrared spectroscopy studies of films of the polypeptides and circular dichroism study of their solutions in hexafluoro-2-propanol and hexafluoropropane-2,2-diol show the tendency of the polypeptides to adopt the beta conformation in the solid state. In pure hexafluoro-2-propanol or hexafluoroacetone, the three polymers adopt what we interpret as random coil conformations. In mixtures of hexafluoro-2-propanol-water or hexafluoropropane-2,2-diol-water, the polypeptide containing the S isomer shows a definite tendency to form beta structure. This tendency is not established for the R and the R,S isomers. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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