7 nm Actin Filament Z-line 1) How many motor molecules matter? In muscle, myosin

Question

7 nm Actin Filament Z-line 1) How many motor molecules matter? In muscle, myosin motor molecules extend from the core of the thick filament binding to sites on actin monomers that comprise the thin filament. The myosin motors are spaced every 43 nm and the actin binding sites the face are spaced every 37 nm (4 pts) M-line 43 n Myosin Filament Titin (a) A myosin motor molecule must be within 2 nm of either side of a binding site to have a reasonable probability of binding. Under this condition, what fraction of myosin motors would actually bind? (show your work) (b) That distance of 2 nm is based on a motor molecule whose spring constant is 5 pN/nm. If the effective spring constant of the motor molecule were doubled, would the fraction of bound cross bridges increase or decrease? (explain your answer

Explanation / Answer

a. in this condition, head part of myosin molecule acually bind to actin filament to rduce the space to 2 mm.

b.yes, as the spring constant increases, the fraction of cross bridges increases. this can be explained as the spacing decreases with the effective spring constant, the binding of myosin head to actin filament increases. More the fraction of binding more is the muscle contraction.

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