Mutation-induced change in chignolin stability from π-turn to α-turn.

ABSTRACT: Chignolin, which consists of 10 amino acids, adopts two stable states in simulations at room temperature at 1 atm: the native and misfolded states. The sequence of chignolin is optimized to form a stable π-turn and thus the native state has a π-turn from Asp3 to Thr8. On the other hand, the misfolded state adopts an α-turn from Asp3 to Gly7. We previously investigated the differences in the stability mechanism of the two states using computational techniques. Our previous detailed energy analysis implied that the native state was stabilized by hydrogen bonding between the side chain atoms of Thr6 and Thr8, and Thr8 was not involved in stabilization of the misfolded state. Thus, we predicted that mutation of Thr8 to a neutral amino acid could stabilize the misfolded structure over the nativ

SUBMITTER: Maruyama Y 

PROVIDER: S-EPMC9054626 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature