A theory of protein spatial-structure evolution in terms of random walks in multidimensional conformational space is proposed. It is shown that the spatial divergence in pairs of homologous proteins depends only on their sequence similarity and is independent of the protein size. X-ray data are reas
Conformation families of protein fragments in multidimensional torsion-angle space
โ Scribed by Pavelcik, Frantisek ;Pavelcikova, Pamela
- Publisher
- International Union of Crystallography
- Year
- 2007
- Tongue
- English
- Weight
- 240 KB
- Volume
- 63
- Category
- Article
- ISSN
- 0907-4449
No coin nor oath required. For personal study only.
โฆ Synopsis
Protein conformation families for automatic model building were determined for dipeptidic, tripeptidic, tetrapeptidic and pentapeptidic fragments. Mapping in n-dimensional conformational space (n = 2, 4 and 6), a conformation-generator method, a deletion-sorting process and a verification procedure were used to calculate the conformational preferences. Torsion angles were harvested from PDB structures with resolutions better than 1.5 A. Statistical weights were calculated for the conformation families.
๐ SIMILAR VOLUMES
Effects of different treatments of the degrees of freedom of bond length stretching and bond angle bending in computational analysis of conformational dynamics of proteins and polypeptides are assessed. More specifically, the normal mode analysis of conformational dynamics of a-helix of deca-alanine