Predicted conformation of poly(dehydroalanine): A preference for turns
| Autor: | Péter Fábián, Virendra S. Chauhan, Sándor Pongor |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
chemistry.chemical_classification
Alanine Molecular Structure Protein Conformation Stereochemistry Biophysics Hydrogen Bonding Peptide Dielectric Biochemistry Molecular mechanics Protein Structure Secondary Solvent chemistry.chemical_compound Crystallography chemistry Structural Biology Dehydroalanine Thermodynamics Molecule Peptides Molecular Biology Conformational isomerism |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1208:89-93 |
| ISSN: | 0167-4838 |
| Popis: | Repetitive conformations of poly(dehydroalanine) were studied using molecular mechanics. An exhaustive search of the conformational space was carried out on a delta Ala octapeptide model, using the AMBER force field and the delta Ala parameters of Alagona et al [26], under three dielectric conditions, epsilon = 1 (vacuum), epsilon = r and epsilon = 4r (solvent). In all cases, two major groups of low-energy conformers were found, one corresponding to a regular 3/10 helix or type III turn, the other to an irregular conformation, phi = -157 to -170 degrees, psi = -1 to 15 degrees which however can be found in the i + 2 position of gamma-turns. The data confirm that delta Ala may induce turn-like structures in peptides and also indicate that it may confer flexibility to the peptide chain. |
| Databáze: | OpenAIRE |
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