Thermal-induced force release in oxyhemoglobin.

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. We have found that around 49 °C oxyhemoglobin crystal samples undergo a sudden and strong increase of their Young's modulus, accompanied by a sudden decrease of the internal friction. This sudden mechanical change (and the ensuing force release) takes place in a partially unfolded state and precedes the full denaturation transition at higher temperatures. After this transformation, the hemoglobin crystals have the same mechanical properties as their initial state at room temperatures. We conjecture that it can be relevant for explaining the oxygen-releasing function of native oxyhemoglobin when the temperature is increased, e.g. due to active sport. The effect is specific for the quaternary structure of hemoglobin, and is absent for myoglobin with only one peptide sequence.

Thermal (in)stability of type I collagen fibrils.

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. For temperatures between 45 and 80 degrees C, the Young's modulus first stabilizes and then increases when the temperature is increased. The hydrated water content and the damping decrement have strong maximums in the interval 70 to 80 degrees C indicating complex intermolecular structural changes in the fibril. All these effects disappear after heat-denaturation of the sample at 120 degrees C. Our main achievement is a five-stage mechanism by which the instability of a single collagen at physiological temperatures is compensated by the interaction between collagen molecules.