Conformational stability of proteins and peptide-peptide interactions in the presence of carbohydrates
β Scribed by G. Barone; P. Del Vecchio; C. Giancola; G. Notaro
- Publisher
- Elsevier Science
- Year
- 1992
- Tongue
- English
- Weight
- 457 KB
- Volume
- 199
- Category
- Article
- ISSN
- 0040-6031
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π SIMILAR VOLUMES
In the native state of proteins there is a marked tendency for an aromatic amino acid to precede a cis proline. There are also significant differences between the three aromatic amino acids with Tyr exhibiting a noticeably higher propensity than Phe or Trp to precede a cis proline residue. In order
## Synopsis A vibrational force field for the polypeptide chain has been developed for normal-mode analysis of such molecules. It can reproduce observed frequencies of known structures to within about 5 cm-l. We review the application of this technique to conformational problems in peptides (@-tur
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