Preceding actin denaturation accelerates myosin denaturation in tilapia myofibrils in frozen storage

Protein denaturation in frozen stored hake (Merluccius merluccius L

Protein solubility of whole and minced muscle of hake (Merluccius merluccius L.) was evaluated at different temperatures of storage: -5°, -12° and -20°C. Proteins soluble in 1% NaCl did not show any change at any of the temperatures of storage, while the 5% NaCl-soluble proteins decreased significantly when whole hake was stored at -5° and 12°C (p < 0.01). A correlation was found between the de...

Reversible denaturation in the myosin adenosine triphosphatase system.

Denaturation and Viscosity of Whey Proteins Solutions as Affected by Frozen Storage

Concentrated solutions of whey proteins (WPC) were prepared from sweet whey by ultrafiltration technique, and stored at – 18°C up to three months. Denaturation degree and viscosity of WPC solutions were assessed. Denaturation degree of whey protein solutions increased significantly (P<0.05) as affected by duration of frozen storage and protein content. The highest degree of denaturation was fou...

Avoiding DNA loss and denaturation upon storage in plastic microtubes

Rotational dynamics of actin-bound myosin heads in active myofibrils.

We have used saturation-transfer electron paramagnetic resonance (ST-EPR) to measure the submillisecond rotational motions of actin-bound myosin heads in active myofibrils. The cross-bridges were spin-labeled with a maleimide nitroxide derivative (MSL) that has previously been shown to undergo microsecond rotational motions on actin-bound myosin heads in solution during steady-state ATPase acti...