In: Biology
You are studying myosin V, a class of myosin which can be used in cells to transport vesicles by “walking” along actin filaments, towards the plus ends of these filaments. You have identified a mutation in the gene for myosin V that affects its ATP binding site. This mutant myosin V (M) can still perform the entire cross-bridge cycle, but it takes much longer to hydrolyze ATP compared to a wild type myosin V (W).
a) Would the duration of the cross-bridge cycle be longer in M or W?Explain?
b) Would the duty cycle (the proportion of the cross-bridge cycle in which myosin is bound to actin) be longer in M or W?Explain?
c) How would this difference in duty cycle affect the ability of M to transport a vesicle along an actin filament? Explain.
The duration of the cross bridge is greater or longer in M as
compared to W. Head of the myosin linked or bind the actin and
pulls the actin filaments towards inwards resulting in the
contraction of muscles. This myosin has also the ATP hydrolysing
property which helps to convert the ATP into ADP and organic
phosphate with release of large amount of energy. This energy is
used to detach the myosin from the actin and this results in the
relaxation of the muscles . The mutant M has defective ATP binding
site . Therefore , the hydrolysing of ATP does not takes place or
it takes place at very slow rate . Therefore due to No or slow
release of energy by the hydrolysis of ATP . The mutant M can still
perform the entire cross bridge cycle phenomenon . But it occurs at
a very slow rates results in the sluggish movement . Contraction of
muscles takes place. Relaxation occurs only by release of energy
that is released by the hydrolysis of ATP molecules. by the ATP
binding site of the myosin. In the relaxed state of the muscles,
the myosin and the actin are seperated. To seperate the myosin and
actin from each other . Certain binding proteins binds to the
myosin binding site on the actin . These proteins are known as
Tropomyosin .
Hence , The cross bridge cycle will be longer in M .
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