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lattice security model - translation to russian
![A schematic of a thermodynamically stable conformation of a generic polypeptide. Note the high number of hydrophobic contacts. amino acid residues are represented as dots along the white line. Hydrophobic residues are in green while polar residues are in blue. See also [https://math.hawaii.edu/~bjoern/?page=labbyfold&string=111111000011000001111000111111&moves=wwwwdssdwwdsssaasdddwwwwdssss&xs=40&ys=40&sheets=1 this example in LabbyFold]](https://commons.wikimedia.org/wiki/Special:FilePath/Thermodynamically Stable Lattice Protein.jpg?width=200 "A schematic of a thermodynamically stable conformation of a generic polypeptide. Note the high number of hydrophobic contacts. amino acid residues are represented as dots along the white line. Hydrophobic residues are in green while polar residues are in blue. See also [https://math.hawaii.edu/~bjoern/?page=labbyfold&string=111111000011000001111000111111&moves=wwwwdssdwwdsssaasdddwwwwdssss&xs=40&ys=40&sheets=1 this example in LabbyFold]")
![A schematic of a thermodynamically unstable conformation of a generic polypeptide. Note the lower number of hydrophobic contacts than above. Hydrophobic residues are in green and polar residues are in blue. See also [https://math.hawaii.edu/~bjoern/?page=labbyfold&string=111111000011000001111000111111&moves=wwwwdssssdwwwwdssssdwwwwdssss&xs=40&ys=40&sheets=1 this example in LabbyFold]](https://commons.wikimedia.org/wiki/Special:FilePath/Thermodynamically Unstable Lattice Protein.jpg?width=200 "A schematic of a thermodynamically unstable conformation of a generic polypeptide. Note the lower number of hydrophobic contacts than above. Hydrophobic residues are in green and polar residues are in blue. See also [https://math.hawaii.edu/~bjoern/?page=labbyfold&string=111111000011000001111000111111&moves=wwwwdssssdwwwwdssssdwwwwdssss&xs=40&ys=40&sheets=1 this example in LabbyFold]")
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Definition
Wikipedia
Lattice proteins are highly simplified models of protein-like heteropolymer chains on lattice conformational space which are used to investigate protein folding. Simplification in lattice proteins is twofold: each whole residue (amino acid) is modeled as a single "bead" or "point" of a finite set of types (usually only two), and each residue is restricted to be placed on vertices of a (usually cubic) lattice. To guarantee the connectivity of the protein chain, adjacent residues on the backbone must be placed on adjacent vertices of the lattice. Steric constraints are expressed by imposing that no more than one residue can be placed on the same lattice vertex.
Because proteins are such large molecules, there are severe computational limits on the simulated timescales of their behaviour when modeled in all-atom detail. The millisecond regime for all-atom simulations was not reached until 2010, and it is still not possible to fold all real proteins on a computer. Simplification significantly reduces the computational effort in handling the model, although even in this simplified scenario the protein folding problem is NP-complete.
