Conformational dynamics of peptide T molecule
| Autor: | Niftali M. Godjayev, Sevim Akyüz, Gulnare Akverdieva |
|---|---|
| Přispěvatelé: | Fen Edebiyat Fakültesi / Faculty of Letters and Sciences Fizik / Physics |
| Rok vydání: | 2002 |
| Předmět: |
chemistry.chemical_classification
Stereochemistry Organic Chemistry Dynamics (mechanics) Peptide T Peptide plane flipping Peptide Conformational entropy Analytical Chemistry Inorganic Chemistry chemistry.chemical_compound Crystallography chemistry Amino acid residue Conformational map Side chain Molecule Spectroscopy |
| Zdroj: | Journal of Molecular Structure. 609:115-128 |
| ISSN: | 0022-2860 |
| DOI: | 10.1016/s0022-2860(01)00974-7 |
| Popis: | Using a method of the theoretical conformational analysis, a conformational dynamics of the side chains of the amino acid residues of peptide T, a competitor of the human immuno-deficiency virus in the binding to human T cells, was investigated. For this purpose, the conformational maps of the potential surfaces were constructed over the angles of the side chains for the preferable conformations of peptide T molecule. Permissible deviations of these angles from the optimal values were determined. It has been found that the angles of the side chains of the amino acid residues involved in physiologically active fragment Thr4-Thr8 are more rigid than in the other segment of the molecule. This fact confirms the existence of such a regular structure as β-turn revealed previously in studies of the spatial structure of the peptide T molecule. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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