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Heavy meromyosin (HMM) is the larger of the two fragments obtained from the muscle protein myosin II following limited proteolysis by trypsin or chymotrypsin. HMM contains two domains S-1 and S-2, S-1 contains is the globular head that can bind to actin while the S-2 domain projects at and angle from (LMM) connecting the two meromyosin fragments. HMM is used to determine the polarity of actin filaments by decorating them with HMM then viewing them under the electron microscope.

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  • Heavy meromyosin (HMM) is the larger of the two fragments obtained from the muscle protein myosin II following limited proteolysis by trypsin or chymotrypsin. HMM contains two domains S-1 and S-2, S-1 contains is the globular head that can bind to actin while the S-2 domain projects at and angle from (LMM) connecting the two meromyosin fragments. HMM is used to determine the polarity of actin filaments by decorating them with HMM then viewing them under the electron microscope. HMM contains 2 binding sites: one for ATP and another for actin filaments. Generally, due to presence of ATP in the HMM, the actin binding site is masked, but during the process of contraction, ATP is hydrolyzed, which unmasks the actin site and thus, myosin head binds with actin forming a cross bridge. (en)
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  • Heavy meromyosin (HMM) is the larger of the two fragments obtained from the muscle protein myosin II following limited proteolysis by trypsin or chymotrypsin. HMM contains two domains S-1 and S-2, S-1 contains is the globular head that can bind to actin while the S-2 domain projects at and angle from (LMM) connecting the two meromyosin fragments. HMM is used to determine the polarity of actin filaments by decorating them with HMM then viewing them under the electron microscope. (en)
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  • Heavy meromyosin (en)
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