Water stabilizes an alternate turn conformation in horse heart myoglobin.

ABSTRACT: Comparison of myoglobin structures reveals that protein isolated from horse heart consistently adopts an alternate turn conformation in comparison to its homologues. Analysis of hundreds of high-resolution structures discounts crystallization conditions or the surrounding amino acid protein environment as explaining this difference, that is also not captured by the AlphaFold prediction. Rather, a water molecule is identified as stabilizing the conformation in the horse heart structure, which immediately reverts to the whale conformation in molecular dynamics simulations excluding that structural water.

SUBMITTER: Bronstein A 

PROVIDER: S-EPMC10102282 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature