Analysis of C‐alpha atom positions from cysteines involved in disulphide bridges in protein crystals shows that their geometric characteristics are unique with respect to other Cys‐Cys, non‐bridging pairs. They may be used for predicting disulphide connections in incompletely determined protein structures, such as low resolution crystallography or theoretical folding experiments. The basic unit for analysis and prediction is the 3 times 3 distance matrix for Cα positions of residues (i – 1), Cys(i), (i + 1) with (j – 1), Cys(j), (j + 1). In each of its columns, row and diagonal vector‐outer distances are larger than the central distance. This analysis is compared with some analytical models.
|Original language||American English|
|Number of pages||10|
|Journal||International Journal of Peptide and Protein Research|
|State||Published - Dec 1987|
- distance geometry
- protein crystallography
- protein folding