Abstract
It is shown that calculation of the thermodynamically stable packing of the protein chain in a domain or in a small globule may be an encompassable task. As an example the search for the most stable packings for amino acid sequences of two β-structural proteins is considered. The approach proposed is based on two physical ideas: 1) use of the molecular field method for organizing an effective sorting of a huge multiplicity of similar structures; and 2) limitation of the set of structures considered solely to those packings of the chain which may prove stable at least for a certain amino acid sequence.
| Original language | English |
|---|---|
| Pages (from-to) | 407-412 |
| Number of pages | 6 |
| Journal | Biophysics (Russian Federation) |
| Volume | 35 |
| Issue number | 3 |
| State | Published - 1990 |
| Externally published | Yes |