Abstract

Interaction between protein and phospholipid molecules in sarcoplasmic reticulum (SR) was studied by measurement of the conformational fluctuation of the protein using the kinetics of the hydrogen-deuterium exchange reaction. It was revealed that the state of SR ATPase undergoes a phase transition at about 18°C with boundary lipids, corresponding to a discrete change in the activation energy of the Ca2+, Mg2+-ATPase reaction.

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