Modeling study on the validity of a possibly simplified representation of proteins.
The folding characteristics of sequences reduced with a possibly simplified representation of five types of residues are shown to be similar to their original ones with the natural set of residues (20 types or 20 letters). The reduced sequences have a good foldability and fold to the same native structure of their optimized original ones. A large ground state gap for the native structure shows the thermodynamic stability of the reduced sequences. The general validity of such a five-letter reduction is further studied via the correlation between the reduced sequences and the original ones. As a comparison, a reduction with two letters is found not to reproduce the native structure of the original sequences due to its homopolymeric features.
Wang
J
J
National Laboratory of Solid State Microstructure and Physics Department, Nanjing University, Nanjing 210093, China.
Wang
W
W
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D007700:Kinetics; D008956:Models, Chemical; D008969:Molecular Sequence Data; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
D000596:Amino Acids; D011506:Proteins