Related Experiment Video
Updated: Aug 2, 2025

Rodent Working Heart Model for the Study of Myocardial Performance and Oxygen Consumption
Published on: August 16, 2016
Water stabilizes an alternate turn conformation in horse heart myoglobin
1Department of Computer Science, Technion-Israel Institute of Technology, Haifa, Israel.
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.
Related Concept Videos
Cooperative Allosteric Transitions
Protein Denaturation
Hemoglobin
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
Imbalances in Cardiac Output
CHF can occur due to the failure of either side of the heart. Left-side failure leads to pulmonary congestion—the right side continues to send...
Protein Folding
Structure of Cardiac Muscles
Compared to skeletal muscles, cardiac muscle cells are small and mostly have a single nucleus. Additionally, they are usually...

