Ontology highlight
ABSTRACT:
SUBMITTER: Bronstein A
PROVIDER: S-EPMC10102282 | biostudies-literature | 2023 Apr
REPOSITORIES: biostudies-literature
Scientific reports 20230413 1
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 imm ...[more]