Publications by authors named "D S Gevorgyan"
Oxygen is released to living tissues via conformational changes of hemoglobin from R-state (oxyhemoglobin) to T-state (desoxyhemoglobin). The detailed mechanism of this process is not yet fully understood. We have carried out micromechanical experiments on oxyhemoglobin crystals to determine the behavior of the Young's modulus and the internal friction for temperatures between 20 °C and 70 °C.
View Article and Find Full Text PDFArticle Synopsis
- Type I collagen is crucial for the structure and strength of connective tissues, but its triple-helical forms are unstable at body temperature, prompting studies on its stability at the fibril level.* -
- Experiments show that heating collagen fibrils causes a decrease in stiffness (Young's modulus) until 58°C, after which stabilization occurs due to intermolecular interactions, alongside water absorption and increased internal friction.* -
- The findings suggest a new intermolecular mechanism for collagen stability, which could enhance our understanding of how these proteins maintain their function in biological tissues.*
We measured the Young's modulus at temperatures ranging from 20 to 100 degrees C for a collagen fibril that is taken from a rat's tendon. The hydration change under heating and the damping decrement were measured as well. At physiological temperatures 25 to 45 degrees C, the Young's modulus decreases, which can be interpreted as an instability of the collagen.
View Article and Find Full Text PDF