An enzyme possesses different kinetics for different substrates as a result of this different products are formed.
Discussion:
- Multi-substrate reactions are governed by intricate rate equations that specify how and in what order the substrates bind. If substrate B is altered while the amount of substrate A remains constant, the study of these reactions becomes considerably easier. The enzyme behaves exactly like a single-substrate enzyme in these circumstances, and a plot of v by [S] yields the actual KM and Vmax constants for substrate B.
- These results can be utilized to determine the reaction's mechanism if a series of such measurements are carried out at various fixed concentrations of A. There are two different sorts of mechanisms for an enzyme that accepts two substrates, A and B, and converts them into two products, P and Q: ternary complex and ping-pong.
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Answer:
Proteins play a fundamental role for life and are the most versatile and diverse biomolecules. They are essential for the growth of the organism and perform a huge amount of different functions.
The passage of DNA to proteins begins with the step of transforming genetic information into an intermediary between DNA and protein. This intermediary is called messenger RNA (mRNA). The difference between DNA and mRNA is that the second corresponds to a very small fraction of all DNA, consists of a single chain (it is no longer a “zipper” but a strand), and that Thymine (T) is replaced by the Uracil (U). This fraction corresponds to the stretch of DNA that contains the sequence necessary to ultimately synthesize the protein.
Answer:
When a muscle cell contracts, the myosin heads each produce a single power stroke.
Explanation:
In rest, attraction strengths between myosin and actin filaments are inhibited by the tropomyosin. When the muscle fiber membrane depolarizes, the action potential caused by this depolarization enters the t-tubules depolarizing the inner portion of the muscle fiber. This activates calcium channels in the T tubules membrane and releases calcium into the sarcolemma. At this point, <em>tropomyosin is obstructing binding sites for myosin on the thin filament</em>. When calcium binds to the troponin C, the troponin T alters the tropomyosin by moving it and then unblocks the binding sites. Myosin heads bind to the uncovered actin-binding sites forming cross-bridges, and while doing it ATP is transformed into ADP and inorganic phosphate which is liberated. Myofilaments slide impulsed by chemical energy collected in myosin heads, <u>producing a power stroke</u>. The power stroke initiates when the myosin cross-bridge binds to actin. As they slide, ADP molecules are released. A new ATP links to myosin heads and breaks the bindings to the actin filament. Then ATP splits into ADP and phosphate, and the energy produced is accumulated in the myosin heads, which starts a new binding cycle to actin. Z-bands are then pulled toward each other, thus shortening the sarcomere and the I-band, and producing muscle fiber contraction.
Answer:
independent: removal of a certain part of the brain
dependent: remembering how to get through the maze
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Answer:
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