Key result
Heating purified rabbit myosin rods causes reversible helical unfolding but irreversible local conformational changes.
Why the study?
The structural thermostability and reversibility of the myosin total rod upon thermal treatment were not fully understood.
Population
Myosin total rod prepared by limited papain digestion of rabbit myosin
Comparison
Thermal treatment (heating) vs cooling after thermal treatment
Design
Preclinical experimental study
Authors
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May indicate undetected functional alterations in myosin despite helix recovery; leaves open relevance to human cardiac stress responses.
The renatured alpha-rope of the myosin total rod exhibits different properties than the native molecule despite no discernible loss in helix content, indicating local irreversible conformational changes.
Samejima et al. (1976) studied this question. Thermal treatment vs. Native (unheated) protein was evaluated on Transition temperature and structural reversibility. Thermal treatment of purified rabbit myosin total rod revealed transition temperatures of 47.5 and 55 °C, with almost full reversibility of helical structure but irreversible local conformational changes.
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