| 초록 |
Two residue beta-turnshave been a major target for engineering protein stability and folding. We attempted to investigate and update the structural and sequence properties of two residue turns in beta-hairpins with a large data set. First, the distribution, dihedral angles and twists of two residue turn types were determined, and compared with previous data. The trend of turn type occurrence and most structural features of the turn types were similar to previous results, but for the first time Type II turns in beta-hairpins were identified. Second, sequence motifs for the turn types were devised based on amino acid positional potentials of two-residue turns, and their distributions were examined. We could identify code-like sequence motifs for the two residue beta-turn types. Finally, we examined the possibility of protein folding control by modulating the in vivo protein folding rate of green fluorescence protein through beta-turn engineering based on the identified code. |
