Unknown

Dataset Information

0

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

altmetric image

Publications

Water stabilizes an alternate turn conformation in horse heart myoglobin.

Bronstein Alex A   Marx Ailie A  

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]

Similar Datasets

| S-EPMC1207205 | biostudies-other
| S-EPMC1959552 | biostudies-literature
| S-EPMC2824769 | biostudies-literature
| S-EPMC1219452 | biostudies-other
| S-EPMC3260668 | biostudies-literature
| S-EPMC3966298 | biostudies-literature
| S-EPMC4702994 | biostudies-literature
| S-EPMC3795489 | biostudies-literature
| S-EPMC3145048 | biostudies-literature
| S-EPMC3797577 | biostudies-literature