What is different about dystrophin in muscles with DMD versus healthy muscles? *
Dystrophin breaks down the lining of the sarcolemma and therefore makes DMD
muscles weak
Dystrophin attaches to enzymes in muscles with DMD and begins the process of
breaking down proteins
An excess of dystrophin in DMD muscles creates chains of proteins that help myosin
attach to actin which contracts the muscle
Dystrophin protein chains are too short in DMD muscles and so does not connect
sarcolemma to the myofibril

Individuals with BMD genetic mutations make dystrophin that is partially functional, which protects their muscles from degenerating as badly or as quickly as in DMD. The dystrophin protein transfers the force of muscle contraction from the inside of the muscle cell outward to the cell membrane.

Explanation:

prophase: we can observe the chromosomes to coil up and condense. they become visible. nuclear membrane and envelope disintigrate.s

metaphase: chromosomes align at the center, the metaphase plate. spindle fibers attach to centromeres of the sister chromatids. they meet at kinetochores.

anaphase: sister chromatids are pulled towards each opposing centromere, set on different poles.

telophase: chromosomes are now clustered up only on either sides of the cell. nuclear membranes reform, and a new cell wall forms along the cell plate. this will lead to cytokinesis, the process that divides the cell membrane and forms the cell wall.